CURRICULUM VITAE

Shagufta Moin, M.D.

DESIGNATION AND PLACE OF WORK Associate Professor

Department of Biochemistry

Jawaharlal Nehru Medical College

Aligarh Muslim University

Aligarh 202002, (U.P.), INDIA. Tel: +91 98 972 17346

Email: shagufta.moin@yahoo.com

HOME/RESIDENCE

44, Sagar Housing Complex

Near CDF P.O., Anoop Shahar Road

Aligarh 202002, (U.P.), INDIA.

Landline No. 0571-2522418

ACADEMIC/EDUCATIONAL QUALIFICATIONS

Qualification Year of Institution award

M.D.(Biochemistry) 1998 J.N. Medical college , A.M.U., Aligarh

Passed in First Attempt

D.G.O. 1994 J.N. Medical college , A.M.U., Aligarh

Passed in First Attempt

M.B.B.S. 1991 J.N. Medical college , A.M.U., Aligarh

All Professionals passed

in First Attempt

Internship 1992 J.N. Medical college , A.M.U., Aligarh

B.Sc. (Hons.) Botany 1985 Women‗s College, A.M.U., Aligarh.

MD Thesis Title: Binding of bilirubin to erythrocytes from healthy smokers and tobacco

chewers.

MCI Registration Number : 10369

Date and Place of Registration : 02.11.1992, New Delhi

1

TEACHING & RESEARCH EXPERIENCE

Designation Institution Duration Particulars of work

Associate Department of Biochemistry August 22, Teaching of M.B.B.S., B.D.S,

Professor J.N. Medical college, 2008 till M.D.S., & Dialysis technique A.M.U., Aligarh date students, guidance of M.D., M.S. and Ph.D. students.

Reader Department of Biochemistry August 22, Teaching of M.B.B.S., B.D.S,

J.N. Medical college , 2005 to M.D.S., & Dialysis technique A.M.U., Aligarh August 21, students, guidance of

2008 M.D.,M.S. and Ph.D. students.

Lecturer Department of Biochemistry December Teaching of M.B.B.S., B.D.S,

J.N. Medical college , 30, 1998 to M.D.S., D.M.L.T., Diploma in A.M.U., Aligarh August 21, Pharmacy & Dialysis technique

2005 students and research.

Demonstrator Department of Biochemistry February 25, Teaching of M.B.B.S., B.D.S,

J.N. Medical college , 1997to Dec M.D.S., D.M.L.T., Diploma in A.M.U., Aligarh 29, 1998 Pharmacy & Dialysis technique

students and research.

B.Sc. (Hons.) Home Science 1st

year (Hygiene and Physiology) 12years

B.Sc. (Hons.) Home Science 2nd

year (Nutritional Biochemistry) 07 years

TOTAL TEACHING EXPERIENCE : over 18 years 10 months

(02years and 01 months as junior resident)

RESEARCH PROJECTS OPERATED/SUBMITTED

PUBLICATION SUMMARY

Published in International Journal : 19

Published in National Journal : 08

International Conferences : 09

National Conferences : 14

Chapter in Books : 01

Communicated to International Journal : 05

Research work presented in International &

National Conferences /Symposium : 29

Training, Refresher, Orientation Courses : 12

Participation in Conference

Workshop, Symposium, CME : 72

Chairing of scientific Session : 02

Invited speaker/ Resource person : 11

2

MAJOR SCIENTIFIC FIELDS OF INTEREST/RESEARCH INTEREST / RESEARCH SPECIALIZATION

Albumin-Bilirubin interaction.

Free radical in health and disease.

Antioxidant and Antiglycation effect of Phytochemicals.

RESEARCH SUPERVISION

Number of student(s) awarded M.D./M.S./M.D.S. degree : 16 Number of student(s) enrolled for M.D./M.S./M.D.S. degree : 04 Number of student(s) awarded Ph.D.degree : 01 Number of student(s) enrolled for Ph.D.degree : 03 Number of student(s) enrolled for M.Phil. : -

Research Guidance Details

(A) M.D./M.S./M.D.S.

S.No. Name of the student Year of Title of Thesis

award

1. Dr. Prince Cheriyan 2003 Clinical, Biochemical and Tumor marker

Modayil, study in malignancy of nose and maxilla.

M.S.[E.N.T.]

(as Co-guide)

2. Dr. Gaurav Kumar 2008 Maternal and fetal indicators of oxidative

Gupta stress in premature/preterm labor.

M.D.[Biochemistry]

3. Dr. Gini Garima 2009 A study on the role of dietary agents in

M.D.[Biochemistry]

protein glycation.

4. Dr. Monal Vashishta 2009 A study of role of oxidative stress markers in

Sharma primary open angle glaucoma.

M.S.[Opthalmology]

(as Co-guide)

5. Dr. Sufia Naseem 2010 Studies on glycated HSA – its implications in

M.D.[Biochemistry]

diabetes mellitus.

6. Dr. Saeeda Wasim 2012 Quantitative evaluation of total antioxidant

M.S.[Obstetrics

capacity (TAC), Malondialdehyde (MDA)

and Thyroid stimulating hormone (TSH)

&Gynaecology]

levels in women with PIH

(as Co-guide)

3

7. Dr. Wajahat Ali Rizvi 2012 Estimation of serum electrolytes(Na+ & K+)

M.S.[Opthalmology]

and serum lipids in patients of senile cataract

and normal individuals of the same age- A

(as Co-guide)

comparative study

8. Dr. Puneet 2012 Comparative study of plasma ascorbic acid

Parasurampuria

and serum nitric oxide levels in senile

cataract patients and normal individuals.

M.S.[Opthalmology]

(as Co-guide)

9. Dr. Namita Gupta 2013 Effect of type 2 diabetes mellitus and

[M.D.S., Perio]dontics

smoking on salivary MMP-8 in chronic

periodontitis patients-A cross sectional study.

(as Co-guide)

10. Dr.Deepti Wadhwa 2013 Determination of levels of Nitric Oxide in

[M.D.S., Periodontics] smoker and non smoker patients with chronic

(as Co-guide) periodontitis.

11. Dr.Ricky Mittal 2014 Biochemical studies on oxidative stress

[M.D.,Biochemistry]

markers in type II diabetics-Role of vitamin

D.

12. Dr.Sushma Sharma 2014 Serum alkaline phosphatase as a bio-marker

[M.D.S.,

of skeletal and dental maturation.

Orthodontics]

(as Co-guide)

13. Dr.Pritma Singh 2014 Impact of smoking and type II diabetes

[M.D.S., mellitus on salivary TNF-alpha level in

,Periodontics] chronic periodontitis patients.

(as Co-guide)

14. Dr.Mohammad Zavir 2014 Evaluation of host factors and identification

Khan of bacterial speceis in patients suffering from

[M.D.S., Oral &

odontogenic infections.

Maxillofascial

surgery]

(as Co- guide)

4

15. Dr.Mazhar Alam 2014 Comparison of serum pro-calcitonin level

[M.D., T.B.

between pulmonary tuberculosis and

community acquired pneumonia.

&Respiratory

diseases]

(as Co-guide)

16. Dr.Humaira Siddiqui 2014 Evaluation of oxidative stress markers in

[M.S. Obstetrics

maternal and cord blood: vaginal delivery

versus elective caesarian section.

&Gynaecology]

(as Co-guide)

17. Dr.Asma Zoya submitted Comparative evaluation of radicular peroxide

[M.D.S.,

penetration from various bleaching agents

during intracoronal bleaching.

Periodontology]

(as Co-guide)

18. Dr.Pankaj Bansal submitted To compare and correlate salivary TNF-alpha

[M.D.S.,

levels in patients with desquamative

gingivitis and chronic gingivitis.

Periodontology]

(as Co-guide)

19. Dr.Kundan Kumar submitted To study the protective effect of olive oil on

[M.S. Anatomy]

the development of atherosclerosis in aorta of

rabbit.

(as Co-guide)

20. Dr.Neha Bansal submitted Evaluation of correlation between vitamin C

[M.D.S., Periodontics]

and total antioxidant capacity in chronic

periodontitis.

(as Co-guide)

(B) Ph.D.

S.No. Name of candidate Year of Title of Thesis

award

1. Miss. Shazia Aman 2014 Antioxidant and antiglycating effect of

phytochemicals.

2. Miss. Naureen Fatima Continuing Functional and clinical relevance of TH-17

cells in diabetes mellitus.

3. Miss. Somaiya Mateen Continuing Role of pro-inflammatory cytokines in

establishment of rheumatoid arthritis.

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LIST OF RESEARCH PUBLICATIONS 1. Role of serum procalcitonin level in differentiating between pulmonary tuberculosis

and community-acquired pneumonia. Mohammad Shameem, Mazhar Alam, Shagufta

Moin, Rakesh Bhargava, Zuber Ahmad, Jamal Akhtar. International Journal of

Clinical Medicine. Vol. 5, pp. 902-909, 2014. [Impact Factor]

2. Segments of spinal cord harboring motor neuron somata of radial nerve of rabbit.

Farhan Kirmani, Nema Usman, Shagufta Moin. Journal of Evolution of Medical

and Dental Sciences. Vol. 3(26) pp. 7112-15, 2014. [Impact Factor]

3. Evaluation of oxidative stress markers in maternal and cord blood: Vaginal delivery

versus Elective caesarean section. Humaira Siddiqui, Nasreen Noor, Shagufta Moin,

Shazia Parveen. International Journal of Current Medical Research. Vol. 3, No. 2,

pp. 024-027, 2014. [Impact Factor]

4. Oxidative stress and antioxidant enzymes in pre-eclampsia. Shazia Parveen, Nasreen

Noor, Shagufta Moin, Zakia Arshad, Naheed Banu. Journal of South Asian

Federation of Obstetrics and Gynecology. Vol. 6(1), pp. 5-7, Jan-Apr, 2014.

5. Serum Na+ and K+ as risk factors in age related cataract: An Indian perspective.

Adeeb Alam Khan, Syed Wajahat A. Rizvi, Abadan K. Amitawa, Shagufta Moin,

Ziya Siddiqui, Faraz Yusuf. Sudanese Journal of Ophthalmology. Vol. 6(1). Jan-

Jun, 2014. [Impact Factor]

6. A study to evaluate the antioxidant and hepatoprotective activity of aqueous extract of

roots of Valeriana wallichii in CCl4 induced hepatotoxicity in rats. S.N. Syed, W.

Rizvi, A. Kumar, A.A. Khan, S. Moin, A. Ahsan. International Journal of Basic

and Clinical Pharmacology. 3(2): 354-358, 2014.[Impact Factor ]

7. Antioxidant and Hepatoprotective Activity of Ethanolic Extract of Valeriana

wallichii in CCl4 treated rats. S.N. Syed, W. Rizvi, A. Kumar, A.A. Khan, S. Moin,

A. Ahsan. British Journal of Pharmaceutical Research. 4(8): 1004-1013, 2014.

8. Study to Evaluate the Antioxidant and Hepatoprotective Activities of Roots Extracts

of Doronicum hookeri in CCl4 Treated Rats. S.N. Syed, W. Rizvi, A. Kumar, A.A.

Khan, S. Moin, and P.A. Khan. European Journal of Medicinal Plants 4(6): 675-

685, 2014

9. In vitro antioxidant and in vivo hepatoprotective activity of leave extract of Raphanus

sativus in rats using CCl4 model. S.N. Syed, W. Rizvi, A. Kumar, A.A. Khan, S.

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Moin, A. Ahsan. African Journal of Traditional Complementary and Alternative

Medicine. 11(3):102-106, 2014. 10. Determination of levels of nitric oxide in smoker & non-smoker patients with chronic

periodotitis : Deepti Wadhwa, Afshan Bey, Mukesh Hasija, Shagufta Moin, Arun

Kumar, Shazia Aman, Vivak Kumar Sharma. J.Periodontal & Implant Science

2013; 43;215-220. [Impact Factor .No impact has been given till date] pISSN 2093-

2278, eISSN 2093-2286

11. Study of serum nitric oxide levels in senile cataract patients and in normal individuals.

Puneet Parasurampuria , Adeeb Alam Khan, Mohammad Ashraf, Shazia Aman and

Shagufta Moin. International Journal of Scientific Research.2013; 2(6):9-11.

[Impact Factor .33] ISSN No 2277-8179

12. Antioxidant activity of thymoquinone and its protective effect against oxidative

haemolysis. Shazia Aman, Shagufta Moin. International Journal of Scientific

Research.2013; 2(4):28-30.[Impact Factor .33] ISSN No 2277-8179

13. Nigella sativa as an antiglycating agent for human serum albumin. Tariq Mahmood,

Shagufta Moin, Abul Faiz Faizy, Sufia Naseem and Shazia Aman. International

Journal of Scientific Research.2013; 2(4):25-27.[Impact Factor .33] ISNN No 2277-

8179

14. Antioxidant activity of thymol: Protective role in AAPH-induced hemolysis in

diabetic erythrocytes. Shazia Aman, Shagufta Moin, M Owais and MU Siddiqui.

International Journal of Pharmaceutical Science Invention.2013; volume 2 issue

3:55-60. [Impact Factor ] ISSN (Online): 2319-6718, ISSN (Print): 2319-670X

15. In vivo study of Histamine H4 receptor in immuno modulation. Tripathi T, Shahid M,

Khan HM, Siddiqui M, Khan RA, Shujat Ullah F, Moin S, Malik A. Bratis Lek

Listy.2012; 113(11):641-7. [Impact Factor .34] pISSN 0006-9248; eISSN 1336-0345

16. Erythrocyte markers of oxidative stress in higher age-group pre-eclamptic and normal

pregnant mothers, Syed K. Haque, M.U. Siddiqui, N. Islam and Shagufta Moin,

Hypertension in Pregnancy 29(1): 69-81 (2010). [Impact Factor 1.52] ISSN: 1064-

1955 print/ 1525-6065 online, cited by 5.

17. Histamine, Histamine Receptors and their Role in Immuno modulation: An Updated

Systematic Review. M. Shahid, T. Tripathi, F. Sobia, S. Moin, M.U. Siddiqui and

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R.A. Khan. The Open Immunology Journal, 2, 9-41 (2009). [Impact Factor .25]

ISSN 1874-2262, cited by 28.

18. Normal delivery induced stress alters glutathione peroxidase and TNF- in elderly

primigravidas mononuclear cells. N. Noor, N. Islam, S. Moin, A.A. Mahdi, S. Jaiswal

and F. Bano. Indian Journal of Clinical Biochemistry, 2008/23 (3), 227-232 (2008).

[Impact Factor .19 ] pISSN 0970-1915, eISSN 0974-0422

19. Tuftsin-mediated immunoprophylaxis against isolate of Aspergillus fumigatus

showing less in vivo susceptibility to amphotericin B. M.A. Khan, N. Ahmad, S.

Moin, A. Mannan, H. Wajahul, S.T. Pasha, A. Khan and M. Owais. FEMS

Immunology and Medical Microbiology, Vol. 44, pp. 269-276 (2005).

Elsevier.[Impact Factor 1.779]

20. Liposome – Bilirubin Interaction: A novel strategy to remove bilirubin from systemic

circulation. M.A. Khan, S. Moin, S. Tayyab, A.F. Faizy, M.U. Siddiqui and M.

Owais. Journal of Liposome Research, Vol. 14, Nos. 3 & 4, pp. 111-122

(2004).[Impact Factor 2.02]

21. Study on Bilirubin Erythrocyte Interaction in diabetic patients. A. Rahman, S. Moin,

M.U. Siddiqui. Indian Journal of Bioresearch, Vol. 50, No. 1, pp. 150-155 (2003).

22. Increased bilirubin binding to erythrocytes of tobacco chewers than non-chewers. S.

Moin, M. Qutub Ali, M.U. Siddiqui and S. Tayyab. Current Science, Vol. 77, No. 2,

25 July (1999). [Impact Factor ]

23. Erythrocytes from healthy smokers bind more bilirubin than the erythrocytes from

healthy non-smokers. S. Moin, M.Q. Ali, M.U. Siddiqui and S. Tayyab. Molecular

and Cellular Biochemistry, 183: 211-214 (1998) Netherlands. [Impact Factor 1.76] ARTICLES PUBLISHED

1. Inherited unconjugated hyperbilirubinemias -A clinical overview.

Shagufta Moin. Indian Journal of Bioresearch. Jan-June 2004; 56(1): 7-9.

2. Programmed Cell Death—Apoptosis, Shagufta Moin. Indian Journal of

Bioresearch.2003; 50(2):74-75

3. Gene Therapy, Shagufta Moin. Indian Journal of Bioresearch. Jan-June 2003;

53(1):44-46.

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4. DNA Vaccines: Designer vaccine for the 21st

century .Shagufta Moin. Indian

Journal of Bioresearch. July-Dec. 2003; 53(2) :158-159. RESEARCH PAPERS ACCEPTED FOR PUBLICATION / COMMUNICATED 1. Serum ALP activity: As a Biomarker of Skeletal And Dental Maturation

Journal of Indian Orthodontic Society (JPJ 1642250714

European Journal of Orthodontics (EJO – 2014- OA 029 )

2. ― Salivary TNF - alpha : A correlation with gingival desquamations‖

Journal of Clinical Periodontology, CPE-11-14-5398

3. Colligation of Total Antioxidant Capacity (TAC) with Periodontal Disease

and

Treatment

Journal of Clinical Periodontology CPE-11-14-5405

4. Unravelling the intricacies of tumor- immune system interrelationships

hindwani

PUBLICATION OF CONFERENCE PRESENTATIONS IN JOURNALS

1. A study on the levels of Antioxidant defense – Enzymes in Pregnancy Induced

Hypertension. S.K. Haque, M.U. Siddiqui, N. Islam and S. Moin. Indian Journal of

Clinical Biochemistry Proceedings. 2007, Vol. 22 (Supl.), ISSN 0970-1915.

2. A study on the levels of Antioxidant defense – Enzymes in Preterm Labour. G.K.

Gupta, N. Islam and S. Moin. Indian Journal of Clinical Biochemistry

Proceedings. 2007, Vol. 22 (Suppl.), ISSN 0970-1915.

3. Effect of EGCG a green tea polyphenol, on the levels of TNF-alpha and glutathione

peroxidase activity in pre-eclampsia patients. R. Alam, S. Moin, N. Noor, G.

Garima, F. Bano and N. Islam. Indian Journal of Clinical Biochemistry

Proceedings. 2007, Vol. 22 (Suppl.), ISSN 0970-1915.

4. Antiglycating Effect of Dietary Agents, S. Moin, N. Noor, R. Alam and S. Khan.

Indian Journal of Clinical Biochemistry Proceedings. 2007, Vol. 22 (Suppl.),

ISSN 0970-1915.

RESEARCH WORK PRESENTED AT CONFERENCES AND SYMPOSIA

1. Naureen Fatima, Shagufta Moin, Nasreen Noor, Humaira Siddiqui. Evaluation of

oxidative stress markers in maternal and cord blood: vaginal delivery verses elective

caesarian section. National symposium on recent advances in free radical biology and

biochemistry under the auspices of UGC-SAP-DRS-III. Department of Biochemistry,

Faculty of Life Sciences. AMU, Aligarh, 06 March 2014.

2. Naureen Fatima, Shireen Hasan, Shagufta Moin, Naheed Banu. Modulatory Role of

Multivitamin Mineral Supplement on Chronic Unpredictable Stress (CUS) and

Dietary Restriction (DR) induced Biochemical Changes in Mice. UGC-SAP

sponsored National Conference on ―Chronic Inflammatory Disorders‖ organized by

D/o Biochemistry, F/o Science & D/o Medical Biochemistry, F/o Medicine (HIMSR)

on Feb 13-15, 2014.

9

3. Ricky Mittal, Shagufta Moin, Neha Mittal. Biochemical Studies on Oxidative Stress

Markers in Type 2 Diabetics- Role of Vitamin D. 3rd

Annual Meeting of the Indian

Academy of Biomedical Sciences & Symposium on Modern Trends in Human

Diseases. Department of Biochemistry, Faculty of Medicine, JNMC, AMU, Aligarh.

14-15 Dec, 2013.

4. Shazia Aman, Shagufta Moin, Mohammad Owais, M. U. Siddiqui. Assessment of

Antioxidant Potential of Eugenol: Its Implications in Diabetes. 3rd

Annual Meeting of

the Indian Academy of Biomedical Sciences & Symposium on Modern Trends in

Human Diseases. Department of Biochemistry, Faculty of Medicine, JNMC, AMU,

Aligarh. 14-15 Dec, 2013.

5. Naureen Fatima, Naheed Banu, Shagufta Moin. Role of Chronic Unpredictable

Stress and Dietary Restriction on Oxidant-Antioxidant Status in Mice. 3rd

Annual

Meeting of the Indian Academy of Biomedical Sciences & Symposium on Modern

Trends in Human Diseases. Department of Biochemistry, Faculty of Medicine,

JNMC, AMU, Aligarh. 14-15 Dec, 2013.

6. Shagufta Moin, Shahnawaz Hasan and Shazia Aman. A study on Oxidative Stress

Markers in Iron Deficient Pregnant Anaemic Women. 21st

Annual Conference of

Medical Biochemists of India, Christian Medical College & Hospital, Ludhiana

(Punjab) 15-17 Nov-2013. 7. Shagufta Moin, Shazia Aman, M. Owais, M.U. Siddiqui, Protective role of Eugenol

against AAPPH induced haemolysis in diabetic erythrocytes, International

Conference on recent advances in diabetes and endocrinology, Rajiv Gandhi Centre

for Diabetes and Endocrinology, Aligarh Muslim University, Aligarh, 15-17 March

2013. 8. Shazia Parveen, Zakia Arshad, Nasreen Noor, Shagufta Moin, Naheed Banu,

Oxidative stress and antioxidant enzymes in pre-eclampsia, International Conference

on recent advances in diabetes and endocrinology, Rajiv Gandhi Centre for Diabetes

and Endocrinology, Aligarh Muslim University, Aligarh, 15-17 March 2013.

10

9. Nasreen Noor, Shahnawaz Hasan, Shazia Aman, Shazia Parveen and Shagufta Moin,

Evaluation of oxidative stress and antioxidant status in iron deficient pregnant anemic

women. International Conference on recent advances in diabetes and endocrinology.

Rajiv Gandhi Centre for Diabetes and Endocrinology, Aligarh Muslim University,

Aligarh, 15-17 March 2013.

10. Shagufta Moin, Shazia Aman, M.Owais, M.U. Siddiqui, Protective effect of

thymoquinone against AAPH induced haemolosis in diabetic erhythrocytes,

International Conference on Chemistry: Frontiers and Challenges, Department of

Chemistry, Aligarh Muslim University, Aligarh, India [Under UGC-SAP(DRS-I)],

March 2-3, 2013.

11. Shagufta Moin, Shazia Aman, M. Owais, M.U. Siddiqui, Assessment of antioxidant

potential of thymol: Its implication in diabetes, International Conference on Advances

in Free Radicals, Redox Signaling and Translational Antioxidant Research and XII

Annual Meeting of the Society for Free Radical Research, India, Organized by CSIR,

Indian Institute of Toxicology Research, Lucknow, Jan. 30 to Feb. 1, 2013.

12. Shazia Aman, M. Owais, M.U. Siddiqui and Shagufta Moin, Evaluation of

Antioxidant activity of Eugenol, International Conference on Advances in Free

Radicals, Redox Signaling and Translational Antioxidant Research and XII Annual

Meeting of the Society for Free Radical Research, India, Organized by CSIR, Indian

Institute of Toxicology Research, Lucknow, Jan. 30 to Feb. 1, 2013.

13. Shagufta Moin, Shazia Aman, M. Owais, M.U. Siddiqui, Evaluation of antioxidant

activity of thymoquinone: Possible role in diabetes mellitus, XX National Conference

of Association of Medical Biochemist of India, Bhubaneshwar, Organized by AMBI

Odisha State Chapter sponsored by UGC, 7-10 December 2012.

14. Shagufta Moin, Shazia Aman, Tariq Mehmood, Evaluation of Antioxidant activity of

Salvadora persica extract, Ist Annual Conference of Association of Physiologists and

Pharmacologists of India UP-UK Chapter, Organized by Department of Physiology

and Pharmacology, J.N. Medical College, AMU, Aligarh,6-7 October 2012.

11

15. Shazia Aman, Tariq Mehmood, Shagufta Moin, Assessment of Antioxidant activity

of Withania somnifera extract, Ist Annual Conference of Association of Physiologists

and Pharmacologists of India UP-UK Chapter, Organized by Department of

Physiology and Pharmacology, J.N. Medical College, AMU, Aligarh,6-7 October

2012. 16. S. Naseem, M.U. Siddiqui, S. Moin, S. Hasan, S. Aman, N. Noor., Glycation of

Human Serum Albumin with Fructose and its implications in Diabetes mellitus,

International Conference on Advances in Free Radicals Research, Natural Products,

Antioxidants and Radioprotectors in Health, Nizam‗s Institute of Medical Science,

Hyderabad and University of Hyderabad, Jan. 11-13, 2010.

17. S. Aman, S. Naseem, S. Moin, M.U. Siddiqui, N. Noor., Biochemical Studies on

Glycated Human Serum Albumin, International Conference on Advances in Free

Radicals Research, Natural Products, Antioxidants and Radioprotectors in Health,

Nizam‗s Institute of Medical Science, Hyderabad and University of Hyderabad, Jan.

11-13, 2010. 18. G. Garima, S. Moin, R. Alam, S. Khan, N. Noor and M.U. Siddiqui, Protective effect

of aged garlic extract in protein glycation, International Conference on Advances in

Free Radical Research and 8th

Annual Meeting of the Society for Free Radical

Research, India, Department of Biochemistry, CSM Medical University, Lucknow

and Era‗s Lucknow Medical College, Lucknow, India, March 19-21, 2009.

19. T. Tripathi, M. Shahid, S. Moin, M.U. Siddiqui and R.A. Khan, Histamine receptors

in immunodulation, 4th

Annual Conference of U.P. Chapter of Indian Association of

Medical Microbiologist UP MICROCON-2008, CSM Medical Univ. Lucknow,

February 16, 2008. 20. S.K. Haque, M.U. Siddiqui, N. Islam and S. Moin, A study on the levels of

Antioxidant Defense Enzymes in pregnancy induced hypertension, 34th

Annual

Conference of Clinical Biochemists of India (ACBI CON-2007), India Habitat Centre,

New Delhi, December 18-20, 2007.

12

21. G.K. Gupta, N. Islam and S. Moin, A study on the levels of Antioxidant Defense

Enzymes in Preterm Labor, 34th

Annual Conference of Clinical Biochemists of India

(ACBI CON-2007), India Habitat Centre, New Delhi, December 18-20, 2007.

22. R. Alam, S. Moin, N. Noor, G. Garima, F. Bano and N. Islam, Effect of EGCG a

Green tea Polyphenol, on the level of TNF- and glutathione peroxidase activity in

Pre-ecclampsie, 34th

Annual Conference of Clinical Biochemists of India (ACBI

CON-2007), India Habitat Centre, New Delhi, December 18-20, 2007.

23. S. Moin, N. Noor, R. Alam, and S. Khan, Antiglycating Effect of Dietary Agents,

34th

Annual Conference of Clinical Biochemists of India (ACBI CON-2007), India

Habitat Centre, New Delhi, December 18-20, 2007. 24. S. Moin, R. Alam and S.Khan, Evaluation of Anti-OxLDL antibodies in pregnancy

induced hypertension, 19th

U.P. Congress of Obstetrics and Gynaecology, Deptt. of

Obs. & Gyn. AMU, November 24 & 25, 2007.

25. S. Moin, M.S. Akhtar and M.U. Siddiqui, Binding of Bilirubin to erythrocytes from

cancer patients, ―International Conference on Anti-oxidants and Free Radicals in

health-nutrition and Radio-protectors‖ & IV Annual Conference of the Society for

Free Radical Research in India (SFRR), St. Johns Medical College, Bangalore,

January 10-12, 2005.

26. S Kumar, M. Aslam and S. Moin, Serum Copper & Serum Amylase Levels in

Nasomaxillary Cancers, Indian Society of Oncology, North Zone Conference, Aligarh

Muslim University, Aligarh, December 20-21, 2003.

27. S. Moin, N. Yusuf, M.U. Siddiqui and N. Islam., The Role of Reactive Oxygen

Species (ROS) in the formation of an alternate autoantigen in the Myocarditis and

DCM, International Conference on Role of Free Radicals and Antioxidants in Health

and Disease 2nd

Annual Conference of SFRR-INDIA, King George Medical College,

Lucknow, February 10-12, 2003.

13

28. A.Rahman, S. Moin and M.U. Siddiqui, Binding of bilirubin to erythrocytes obtained

from diabetic patients, International Conference on Role of Free Radicals and

Antioxidants in Health and Disease 2nd

Annual Conference of SFRR-INDIA, King

George Medical College, Lucknow, February 10-12, 2003.

29. S. Moin, M.Q. Ali, S. Tayyab and M.U. Siddiqui, Binding of bilirubin to erythrocytes

from healthy smokers and non-smokers, 65th

Annual Meeting of the Society of

Biological Chemists, India, Indian Institute of Science, Bangalore, November 20-23,

1997.

CHAIRING OF SCIENTIFIC SESSIONS

Chaired a session in the National Symposium on Emerging Trends in Biological

Sciences: Special Emphasis on Neurosciences, 24-25 September, 2012. Organized by

Interdisciplinary Brain Research Centre, Faculty of Medicine, J.N.M.C., A.M.U.,

Aligarh

Chaired a session in the 3rd

Annual Meeting of the Indian Academy of Biomedical

Sciences & Symposium on Modern Trends in Human Diseases, December 14

&15,2013. Organized by Department of Biochemistry Faculty of Medicine, J.N.M.C.

,A.M.U.,Aligarh BOOK CHAPTERS: Chapter contributed in the book Biomedical Aspects of Histamine: New Perspectives published by Springer.

Possible Effect of Histamine in Physiology of Female Reproductive Function – An

Updated Review. N. Noor, T. Tripathi, S. Moin, A.F. Faizy. Biomedical Aspects of

Histamine: New Perspectives (Springer) 2010.

14

INVITED SPEAKER / RESOURCE PERSON

1. Faculty in U.G. Orientation Programme held at J.N. Medical College, AMU,

Aligarh, 1st

and 2nd

Sep, 2014.

2. Invited as a faculty to participate in Validation /Moderation Workshop of MCQ

Question Bank on 26 & 27 August 2014 at NBE Office, Dwarka, New Delhi. Ref No

NBE/VAL-WORKSHOP/MCQ/AUG/2014/102.

3. Delivered a lecture in Interdisciplinary Subject Refresher Course in Environmental

Studies at UGC Academic Staff College on Teaching Skills, 21.08.2014. .

4. Delivered a lecture in Interdisciplinary Subject Refresher Course in Environmental

Studies at UGC Academic Staff College on Ultraviolet rays (UV rays) - Some

interesting facts , 14.08.2014.

5. Delivered a lecturer in P.G. Orientation Programme on Teaching Skills at J.N.

Medical College, AMU, Aligarh, 01 July 2014.

6. Delivered a lecture in Interdisciplinary Subject Refresher Course in Environmental

Studies at UGC Academic Staff College on Sunshine & Strong Bones, 17.05.2012 .

7. Delivered a lecture in Interdisciplinary Subject Refresher Course in Environmental

Studies at UGC Academic Staff College on Sunshine & Strong Bones, 15.05.2012.

8. Delivered a lecture in Interdisciplinary Subject Refresher Course in Environmental

Studies at UGC Academic Staff College on Biochemical changes in humans due to

UV rays exposure, 28.07.2010.

9. Delivered a lecture in FOGSI Postgraduate CME on HIV in Pregnancy in the

Department of Obstetrics and Gynaecology, J.N. Medical College, AMU, Aligarh, 13

December 2009.

10. Delivered a lecturer in P.G. Orientation Programme on Rational Use of Laboratory

Investigations (Biochemical) at J.N. Medical College, AMU, Aligarh, 20 August

2009.

11. Delivered a Lecture on Water and Water Born Diseases in the Department of

Geography, AMU, Aligarh to the participants of Refresher course, 28 March 2003.

15

SEMINAR / SYMPOSIUM / CME / WORKSHOP / CONFERENCES ATTENDED 1. National CME on ―Pharmacotherapy Update in Common Medical Disorders- A Rational

Approach‖ organized by Department of Pharmacology, J.N. Medical College, AMU,

Aligarh. Nov. 1-2, 2014. 2. CME on Managing Medical Records ―Embedding Substantial Potential Benefit into

Practice‖ organized by Central Record Section of J.N. Medical College and Hospital,

AMU, Aligarh, 12th

May, 2014. 3. CME on ― Rational use of Blood Components‖, Department of Pathology, J. N. Medical

College and Hospital. 24 th

March 2014. 4. CME on Central Sterilization Services Principles and Practice, organized by J. N. Medical

College and Hospital, A.M.U., Aligarh. 22 nd

March 2014. 5. National Workshop cum CME on Alternatives to Animal Experimentation in Medical

Science Education ( partially sponsored by MCI), Department of Pharmacology, J.N.

Medical College, A.M.U., Aligarh. 24-25 February 2014.

6. 3rd

Annual Meeting of the Indian Academy of Biomedical Sciences & Symposium

on Modern Trends in Human Diseases, December 14 &15,2013. Organized by

Department of Biochemistry Faculty of Medicine, J.N.M.C. ,A.M.U., Aligarh.

7. 21st

Annual Conference of Association of Medical Biochemists of India,held at

Christian Medical College,Ludhiana 15th

-17th

November, 2013. 8. Workshop on ―Soft Skills in Medical Education‖organized by Christian

Medical College Ludhiana on 14-11-2013. 9. Hands on Workshop on ―How to write and Publish a case report‖ organized by

Department of Medicine, Jawaharlal Nehru Medical College, A.M.U., Aligarh in

scollaboration with ‗ BMJ Case Reports‗ on 14-08-2013. 10. International Conference on Recent Advances in Diabetes and Endocrinology, 15-17

March, 2013 organized by Rajiv Gandhi Centre for Diabetes and Endocrinology,

Aligarh Muslim University, Aligarh in collaboration with Indraprastha Apollo Centre for

Obesity, Diabetes and Endocrinology. 11. International Conference on Chemistry: Frontiers and Challenges, March 2-3, 2013,

Department of Chemistry, Aligarh Muslim University, Aligarh, India [Under UGC-SAP

(DRS-I)]. 12. Foundation Day Symposium on Current Trends in Biotechnology, Jan. 16, 2013

organized by Interdisciplinary Biotechnology Unit, AMU, Aligarh.

16

13. International Conference on Advances in Free Radicals, Redox Signaling and Translatinal

Antioxidant Research in XII Annual Meeting of the Society for Free Radical Research-

India, Jan. 30 to Feb. 1, 2013 organized by: CSIR-Indian Institute of Toxicology

Research, Lucknow. 14. XX National Conference of Association of Medical Biochemists of India, organized by

AMBI Odisha State Chapter sponsored by UGC.

15. 1st

Annual Conference of Association of Physiologists and Pharmacologists of India,

UP-UK Chapter, jointly organized by Department of Physiology and Pharmacology, J.N.

Medical College, AMU, Aligarh. 16. National Symposium on Emerging Trends in Biological Sciences: Special Emphasis on

Neurosciences, 24-25 September, 2012 organized by Interdisciplinary Brain Research

Centre, Faculty of Medicine, A.M.U., Aligarh. 17. Popular Lectures on Neuroscience and Nanotechnology (A DBT funded Programme)

organized by Interdisciplinary Brain Research Centre, (IBRC) Faculty of Medicine,

AMU, Aligarh, 29 December 2012. 18. Symposium cum live workshop on Chronic Back Pain organized by Department of

Anaesthesiology and Critical Care, J.N. Medical College, AMU, Aligarh in Association

with Indian Society for Study of Pain, 22 Dec. 2012.

19. National Symposium on Medical Ethics: Challenges and Future Prospects, 9th

Sept.

2012, Medical Education Unit, Faculty of Medicine, AMU, Aligarh. 20. Golden Jubilee CME on metamorphosis: Channelling the change for betterment of

Medical Education in India, 31st

Mach 2012, Medical Education Unit, Faculty of

Medicine, AMU, Aligarh. 21. Silver Jubilee Symposium on Emerging Trends in Biochemical and Toxicological

Sciences, Department of Biochemistry, Faculty of Life Sciences, A.M.U., Aligarh,

March 06, 2012.

22. 23rd

Annual Conference of UP Chapter of Obstetrics and Gynaecology of India, 19-20

November, 2011 organized by Agra Obstetrics & Gynaecology Society and Department

of Obs. & Gynae. S.N. Medical College, Agra. 23. Scientific Programme on Pharmacovigilance conducted by Knowledge Academy on 17

November 2011, J.N. Medical College, A.M.U., Aligarh.

24. Symposium on Emerging Trends in Dengue and other haemorrhagic fevers in India, 8th

October 2011 organized by Department of Microbiology, J.N. Medical College,

A.M.U., Aligarh. 17

25. Workshop on Student Assessment, 7-8 March 2011, Medical Education Unit, Faculty of

Medicine, AMU, Aligarh. 26. International Conference on Chemistry: Frontiers and Challenges, 5-6 March 2011,

Department of Chemistry, AMU, Aligarh. 27. National Symposium on Current Trends and Biochemical, Biomedical, and

Environmental Sciences, 22 February 2011, Department of Biochemistry, Faculty of

Life Sciences, AMU, Aligarh.

28. International Conference of Integrative Medicine and 1st

SAARC Conference of Unani

Medicine, 2-4 February 2011 organized by Faculty of Unani Medicine, AMU, Aligarh. 29. Malaria – An update organized by Department of Microbiology, J.N. Medical College,

A.M.U., Aligarh, 18 December 2010.

30. AMBICON-2010, 18th

National Conference of Association of Medical Biochemist of

India, Hyderabad, 12-14 November, 2010. 31. Workshop on Techniques in Haemoglobinopathies, 11 November 2010 at Tapadia

Diagnostic Centre, Hyderabad. 32. Faculty Development Programme on Medical Education Technology, 05.04.2010, J.N.

Medical College, AMU, Aligarh. 33. National Symposium on Sports Physiology Today and Tomorrow organized by

Department of Physiology, J.N. Medical College, AMU, Aligarh. 34. FOGSI Postgraduate CME, Department of Obstetrics and Gynaecology, JNMC, AMU,

Aligarh, December 13, 2009. 35. Scientific Programme on Basics of Clinical Research, Piramal Knowledge Academy,

Medical Education Unit, JNMC, AMU, Aligarh, December 8, 2009. 36. CME LIFE (Let Induction Fulfill Existence), AOGS, Department of Obstetrics and

Gynaecology, JNMC, AMU, Aligarh, October 3, 2009. 37. CME Gynae Endocrinology, under aegis of FOGSI and DST, Department of Obstetrics

and Gynaecology, AIIMS, New Delhi, April 18, 2009. 38. International Conference on Advances in Free Radical Research, Natural Products,

Antioxidants and Radio-protectors and 8th

Annual Meeting of the Society for Free

Radical Research India, Department of Biochemistry, C.S.M. Medical University &

Eras Lucknow Medical College, Lucknow, March 19-21, 2009. 39. International SFRR Satellite Symposium 2009 on Free Radicals in Health and Disease,

Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University,

Aligarh, March 17-18, 2009.

18

40. CME Programme on Role of Letrazole in Ovulation Induction, Department of Obstetrics

and Gynecology, J.N. Medical College, A.M.U., Aligarh, Feb. 21, 2009. 41. Orientation and Sensitization Workshop on Science Writing/Journalism, National

Council for Science and Technology Communication, DST, New Delhi, Department of

Mass Communication, AMU, Aligarh, December 6-10, 2008. 42. Continuing Medical Education and Workshop-2008 on Mechanical Ventilation and ABG

Analysis in Association with Indian Society of Critical Care Medicine, Department of

Anaesthesiology and Critical Care, JNMC, AMU, Aligarh, December 12, 2008. 43. National Symposium on Advances in Clinical Biochemistry Biomarkers, Molecular

Diagnosis and QUALITY Diagnosis and Quality Assurances & 1st

U.P. Chapter of

Association of Clinical Biochemists of India (UPACBICON), Department of

Biochemistry, J.N. Medical College, AMU, Aligarh, November 15-16, 2008. 44. Interdisciplinary Science Conference-2008 Mathematics in Biology, Centre for

Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi. 45. National Workshop on Prevention of Lead Poisoning, Department of Biochemistry,

C.S.M. Medical University, Lucknow, 29th

March 2008. 46. Molecular Medicine Update – 2008, Maulana Azad Medical College, Delhi, March, 28,

2008. 47. International Symposium on the Predictive, Preventive and Mechanistic Mutagenesis

and XXXIII EMSI Annual Meeting, EMSI, Department of Agriculture, AMU, Aligarh,

January 1-3, 2008.

48. 34th

Annual Conference of Clinical Biochemistry of India, ACBICON-2007, New Delhi,

December 18-20, 2007. 49. CME & Workshop on Stem Cell Therapy, Escort Heart Institute and Research Ltd., New

Delhi, December 17, 2007.

50. 19th

U.P. Congress of Obstetrics and Gynaecology, UPCON-2007, Obstetrics and

Gynaecology Society, J.N. Medical College, AMU, Aligarh, November 24 & 25, 2007. 51. CME on HIV/AIDS Prevention and Treatment Awareness, National AIDS Control

Organization and Indian Medical Association, April 22, 2007. 52. National Symposium on Relevance of Pharmaco-Vigilance for Indian Systems of

Medicine, Under the aegis of Society of Pharmaco-Vigilance, India, Department of

Pharmacology, J.N. Medical College, A.M.U., Aligarh, November 4, 2006.

19

53. ICOG CME on Ultrasound and Cardiotocography, Aligarh Obstetrics and Gynaecology

Society (AOGS), Department of Obstetrics and Gynaecology, J.N. Medical College,

AMU, Aligarh, March 2, 2006. 54. XIV Annual Conference of Indian Association of Pathologists and Microbiologists (U.P.

Chapter), Department of Pathology, J.N. Medical College, AMU, Aligarh, November

23, 2005. 55. Workshop on Colposcopy and Management of Cervical Pre-cancer, Department of

Obstetrics and Gynaecology, J.N. Medical College, AMU, Aligarh, March 20-21, 2005. 56. International Conference on ―Antioxidants and Free Radicals in Health-Nutrition and

Radioprotectors‖ and IV Annual Conference of SFRR-India, Department of

Biochemistry, St. John‗s National Academy of Health Sciences, January 10-12, 2005. 57. Cardio Diabetology Update-2004, Endocrinology Division, Department of Medicine, J.J.

Medical College, AMU, Aligarh, October 9-10, 2004. 58. ISO, North Zone Confernece-2003, Indian Society of Oncology, Department of

Radiotherapy, J.N. Medical College, AMU, Aligarh, December 20-21, 2003. 59. CME Programme, Indian Society of Anaesthesiologist/WFSA, J.N. Medical College,

AMU, Aligarh, November 29-30, 2003. 60. North Zone CME in Endocrinology, Endocrine Society of India, MCI, J.N. Medical

College, AMU, Aligarh, September 15-16, 2003. 61. Live IUI Workshop, Aligarh Obstetrics and Gynaecology Society, Department of

Obstetrics and Gynaecology, J.N. Medical College, AMU, Aligarh, May 11, 2003. 62. Issues in Medicine - An Update, Department of Medicine, J.N. Medical College, AMU,

Aligarh, March 29-30, 2003. 63. International Conference on Role of Free Radicals and Antioxidants in Health and

Disease and 2nd

Annual Conference of SFRR-INDIA, Department of Biochemistry,

C.S.M. Medical University, Lucknow, February 10-21, 2003. 64. Indo-US Workshop on Problem Based Learning in Medical Education, J.N. Medical

College, AMU, Aligarh, November 21, 2001. 65. Reproductive and Child Health Workshop, Aligarh Obstetrics and Gynaecological

Society in Collaboration with Federation of Obstetrics and Gynaecological Societies of

India and MOHFW, Govt. of India and WHO, J.N. Medical College, AMU, Aligarh,

September 22-23, 2001. 66. Bioinformatics Workshop on Information Retrieval through Internet for the study of

Protein Structure and Other Applications, Department of Biochemistry, Ministry of

20

Science and Technology, Govt. of India, New Delhi, Distributed Information Sub-

Centre, Biotechnology Building, AMU, Aligarh, January 9-11, 2001.

67. 10th

Annual Conference, U.P. Chapter of Obstetrics and Gynaecology, Aligarh Obstetrics

and Gynaecological Sociewty, J.N. Medical College, AMU, Aligarh, November 22-23,

2007. 68. Introduction to the use of Personal Computers and Window Based Softwares in

Bioinformatics with Special Reference to NICNET Connectivity and CD-ROM

Databases, Department of Biochemistry, Ministry of Science and Technology, Govt. of

India, New Delhi, Distributed information Sub-Centre, Biochemistry Building, AMU,

Aligarh, March 10-12, 1997.

69. 65th

Annual Meeting of the Society of the Biological Chemists (India), Department of

Biochemistry, Indian Institute of Science, Bangalore, November 20-23, 1996. 70. Workshop on Advanced Gynecological Endoscopy, Department of Obstetrics and

Gynecology, J.N. Medical College, AMU, Aligarh, July 26-27, 1994. 71. Mid-Term Endocrine Conference and CME, Endocrinology and Metabolic Section,

Department of Medicine, J.N. Medical College, AMU, Aligarh, July 26-27, 1994. 72. Comprehensive Postgraduate Teaching Course (CME), under the auspices of AOGD,

Department of Obstetrics and Gynaecology, UCMS and GTB Hospital, Delhi, April 16-

17, 1994.

TRAINING / REFRESHER / ORIENTATION / PROFESSIONAL COURSES ATTENDED

1. MCI Advance Course in Medical Education held from 29th

Sep 2014 – 2nd

Oct 2014

at MCI Nodal Centre for Faculty Development, NHL Municipal Medical College,

Ahemdabad.

2. Medical Council of India, Basic Course Workshop in Medical Education

Technologies, held by the Regional Centre Maulana Azad Medical College, New

Delhi during 29 April- 02 May 2014.

3. Short Term Course on Academic Paper Writing Skills held at UGC Academic Staff

College,AMU, Aligarh from 26 th

March – 02 nd

April 2014.

4. Training course on Application of Research Techniques in Reproductive Biomedicine

held at NIHFW, New Delhi from November 16-27, 2009.

21

5. Subject Refresher Course in Computer Applications (Interdisciplinary) held at UGC

Academic Staff College, AMU, Aligarh from December 21, 2008 to January 21,

2009.

6. Professional Course in Clinical Biochemistry organized by Escorts Heart Institute and

Research Centre Ltd., New Delhi from December 15-16, 2007.

7. Annual Training Course in Endocrinological Techniques and their Applications held

at National Institute of Nutrition, Hyderabad from August 21 to September 29, 2006.

8. 49th

National Teacher Training Course on Educational Science Technology for

Teachers of Health Professionals held at National Teacher Training Centre,

Department of Medical Education, Maulana Azad Medical College, New Delhi from

January 27, 2003 to February 05, 2003.

9. Training Course on Molecular Biology, Hybridoma and Cell Culture Techniques

conducted at National Biotechnology Centre, Indian Veterinary Research Institute,

Izatnagar from September 08-29, 2003 under the auspices of National Agricultural

Technology Project (NATP) on Human Resource Development in Veterinary

Biotechnology.

10. District Level Training of Trainers on HIV/AIDS conducted by JNMC, AMU,

Aligarh under the auspices of U.P. State AIDS Control Society, Nawal Kishore Road,

Lucknow from April 08-10, 2002.

11. Refresher Course in Biochemistry held at UGC Academic Staff College, AMU,

Aligarh from October 15 to November 06, 2001.

12. Orientation Programme in Biochemistry held at UGC Academic Staff College, AMU,

Aligarh from November 07 to December 07, 2001.

APPOINTED AS M.D., M.B.B.S., B.D.S., M.Sc.(Clinical Biochemistry), M.Sc.(Medical Biochemistry), B.Sc.(Home Science) EXAMINER

1. M.D., M.B.B.S., B.D.S. J.N. Medical College, A.M.U. Aligarh, U.P.

2. B.Sc. Hons.(Home Science), Women,s College, A.M.U. Aligarh, U.P.

3. M.B.B.S., S.N. Medical College, Agra, U.P.

4. M.B.B.S., Rohilkhand Medical College, Bareilly, U.P.

5. M.B.B.S., Sri Ram Murti Smarak Institute of Medical Sciences, Bareilly.U.P.

6. M.B.B.S., National Institute of Medical Sciences, Jaipur, Rajasthan.

7. M.B.B.S.& M.D., Himalayan Institute of Medical Sciences,Dehradun, Uttarakhand,

8. M.B.B.S., Subharti Medical College, Meerut, U.P.

22

9. M.B.B.S., Lala Lajpat Rai Memorial Medical College, Meerut,U.P.

10. B.D.S.&M.Sc.(MedicalBiochemistry),Teerthankar Mahavir University, Moradabad

U.P.

11. M.Sc. (Clinical Biochemistry), University of Kashmir, Srinagar.

12. M.B.B.S., All India Institute of Medical Sciences,Rishikesh,Uttarakhand.

13. M.B.B.S. and M.Sc.(Medical Biochemistry) Integral University , Lucknow , U.P.

APPOINTED AS PAPER SETTER

M.B.B.S., B.D.S.and M.Sc. (Medical Biochemistry), Teerthankar Mahavir University,

Moradabad, U.P.

Ph.D.entrance,Ph.D.CourseWork(PrePh.D).,&M.Sc.(MedicalBiochemistry),IntegralU

niversity,Lucknow, U.P.

M. D. Biochemistry, Rohilkhand University, Bareilly.

ADMINISTRATIVE RESPONSIBILITIES

Member of Committee to monitor overall cleanliness and ambience in the department.

Member of undergraduate and postgraduate syllabus revision committee.

Treasurer National CME on ―Pharmacotherapy Update in Common Medical

Disorders- A Rational Approach‖ organized by Department of Pharmacology, J.N.

Medical College, AMU, Aligarh. Nov. 1-2, 2014.

Member of reception and registration committee for National Symposium on

―Hospital Acquired Infections & Antimicrobial Resistance‖ held on 9th

Dec, 2014.

Warden, S.N. Hall, September 16, 2000 to June 2007.

Incharge Clinical Lab. of the Department of Biochemistry, ( 2000-2003).

Incharge for M.D. Seminar Lectures since October 2005.till date.

Scrutinizer for compulsory retotalling /scrutiny of marks for session 2013-14.

23

MEMBERSHIP/PARTICIPATION IN BODIES/COMMITTEES ON EDUCATION

Member, Executive Committee, FOGSI ( Aligarh Branch ).2005-2008 & February

2012 till date.

Member of the Faculty of Medicine, A.M.U. Aligarh for a period of two years w.e.f.

Appointed as Member of Board of Studies, Department of General Human

Physiology & Biochemistry, Teerthankar Mahavir University, Moradabad for a period

of two years w.e.f. 2009-2011.

Member of the Faculty of Medicine, w.e.f. from 29-8-2013 for a period of two years.

Member of Medical Education Unit, J.N. Medical College, A.M.U., Feb 2014.

CO-CURRICULAR ACTIVITIES

Active participation as Judge for various cultural and sport events during S.N. Hall

week celebration

Deputed to Jeddah as Lady Medical Officer to Indian Medical Mission Hajj in

1998, 1999 and 2002.

Participated in TV Shows on ETV Urdu e.g. ―Bazm-e-Niswan‖, Hajj Ek Ibadat,

Sehri Times, Tandrusti Hazar Niyamat, Quiz Line and Adaab Doctor.

Worked in a project entitled ―Epidemiological studies of Radiation Occupational

Workers and their Families at Atomic Power Project/Station Sites Nuclear

Power Corporation, Govt. of India (1996).

OUTREACH ACTIVITIES

Participated as a specialist in several health camps in and around Aligarh.

Participated in Pulse Polio Programme-2000

REVIEWER OF PAPERS Reviewed the papers for the following journals-

Indian Journal of Biochemistry and Biophysics

International Journal of Medicine and Medical Sciences

Biomed Research International 24

EDITORIAL MEMBERSHIP

Registered in the editorial board as Advisory board for the Journal BP J00000 232- International Journal of Medical and Clinical Research. LIFE MEMBERSHIP OF NATIONAL AND INTERNATIONAL SCIENTIFIC

BODIES /SOCIETIES

Life Member of the Society of Biological Chemists, India. Life Membership No.

1261 (2000).

Life Member of Association of Clinical Biochemists of India 2007. Life

Membership No. 2934.

Life Member of U.P. Chapter of Obstetricians and Gynaecologists from November

2007.

Life Member of Indian Medical Association. Membership No. UP/8467/2/174/

143865/2009-10/L (2009).

Life member of the Society of Biological Scientist of India from 20.02.2010,

Membership No. LM/SBSI/134.

Life member of the Association of Medical Biochemists of India. Membership No.

UP-05.

Member of the International Association of Lions Club ( Aligarh branch).

Life member of Indian Academy of Biomedical Sciences (IABS). Membership

number 96/2012

Life member of Indian Society for Lead Awareness & Research. Membership

number 29/2012

25

PARTICIPATION IN HEALTH SHOWS ON TELEVISION

From 2005 to 2010 participated as an Expert every year in the ―SEHRI TIME”,

Sehri Time is a Live Phone in show which telecast daily on ETV Urdu in the holy

month of RAMADHAN. If viewers have any query about any medical problem,

expert present in the studio give the answers of their problems. I participated as a

Gynaecologist and Medical Practitioner in two episodes every year. The programme

aired from 4:00 am to 5:00 am.

ETV Urdu airs another special show for Hajj Pilgrims on the occasion HAJJ. This is a

live phone in show titled ―HAJJ EK IBADAT‖ in which different Islamic scholars

along with medical experts, who have performed Hajj, give the answers of the

pilgrims. Since I was the part of Hajj Delegation in 1998, 1999 and 2002, I

participated as an Medical Practitioner and share my experiences on different aspects

of health and also give the answers of the questions of the pilgrims related to health

and care to be taken during Hajj. I was participating every year in two episodes from

2005-2006.

Participated as an Obstetrician and Gynaecologist in several episodes of

―TANDRUSTI HAZAR NIYAMAT‖ – a health based show on ETV Urdu. The

topics on which I participated was Breast Feeding, Antenatal and Postnatal Care,

Ovulation, Infertility, Women‗s Health, Tobacco Control, Nutrition in Pregnancy,

Contraceptives etc.

Actively involved in Live phone in health show on ―ETV Urdu‖, titled ―AADAB

DOCTOR‖. Adab Doctor is a bi-weekly show, in which different health related issues

are discussed and viewers in more than 52 countries ask their query about any medical

problem, to get the answers from the experts present in the studio. The programme

airs every Thursday and Friday from 5:00 to 6:00 pm. More than 125 episodes have

been telecast till date.

Actively involved for another Live Quiz Based show on ETV Urdu titled “QUIZ

LINE”. The programme is designed by keeping in mind the students upto Senior

Secondary Level. There are more than 20 topics on which questions are asked, the

subjects which I am handling are Science and Technology, The programme airs Every

Sunday from 10:30 pm to 11:30 pm.

26

PERSONAL DETAILS

Father‗s Name : Mr. Moind Uddin

Mother s Name : Mrs. Nafees Moin

Nationality : Indian (Passport No. )

Date of Birth : November 01, 1965

Marital Status : Married

Languages : English, Urdu, Hindi

REFEREES

1. Prof. M.U. Siddiqui Department of Biochemistry , Faculty of Medicine Aligarh Muslim University,Aligarh-202 002 (INDIA) E-mail: mashiat2000@rediffmail.com Phone No.: 09837201776

2. Prof. Saad Tayyab Institute of Biological Sciences, Faculty of Science Building, University of Malaya 50603, Kuala Lumpur ,(MALAYSIA) E-mail: saadtayyab2004@um.edu.my Phone No.: 03-79677118 (office) Fax: 03-79674178

Teaching Material on

“Enzymes” for MBBS First

Professional Students, 2014 Batch

ENZYMES

Biologic polymers that catalyze chemical reactions that

make life possible.

BIOMEDICAL IMPORTANCE

Presence & maintenance of a complete & balanced set of

enzymes is essential for the breakdown of nutrients to

supply energy & chemical building blocks. These building

blocks assemble into proteins, DNA, membranes, cells &

tissues. Energy harnessed is used to power cell motility,

neural functions & muscle contraction.

The ability to assay the activity of specific enzymes in

blood, other tissue fluids or cell extracts aids in diagnosis

& prognosis of disease.

Enzymes can be employed in the clinical laboratory as

tools for determining critical metabolites e.g. glucose

oxidase is frequently utilized to measure plasma glucose

concentration.

Enzymes are also employed as tools for treatment of

injury & disease. Tissue plasminogen activator, or

streptokinase is used in the treatment of MI while trypsin

has been used in the treatment of cystic fibrosis.

Sensitivity of enzyme assays can be exploited to detect

proteins that lack catalytic activity in ELISA.

A complete balanced set of enzyme activities is of

importance for maintenance of homeostasis.

They are targets of choice for drugs that cure or

ameliorates human disease. Defective enzymes/ deficiency

in the quantity or catalytic activity of key enzyme can

result from genetic defects/ genetic mutations, nutritional

deficits or toxins/ infections by viral or bacterial

pathogens (e.g. vibrio cholerae)

INDUSTRIAL USES

Proteases & amylases augment the capacity of detergents

to remove dirt & stains.

Enzymes also play a role in producing or enhancing the

nutrient value of food products for both humans &

animals. The protease renin, for e.g. is utilized in the

production of cheese, while lactose is employed to remove

lactose from milk for the benefit of lactose-intolerant

persons deficient in this hydrolytic enzymes.

PROPERTIES OF ENZYMES

Enzymes catalyze conversion of one or more compounds

(substrates) into one or more different compounds

(products). They possess two important properties-

EFFICIENCY- enhance the rate of corresponding non-

catalyzed reaction by factors of atleast 106

SPECIFICITY- they are specific both for the type of

reaction catalyzed & for a single substrate or a small set of

closely related substrate. Enzymes are also stereo-specific

catalyst & catalyze reactions of only one stereo-isomer of

a given compound. For e.g. D- but not L- sugars, L- but

not D- amino acids.

Most of the enzymes are proteins, exceptions include

ribosomal RNAs, & self-cleaving or self-splicing RNA

molecules known collectively as ribozymes.

CO-FACTORS, CO-ENZYMES, PROSTHETIC

GROUPS

Many enzymes contain small non-protein molecules &

metal ions that participate directly in substrate binding &

catalysis. They are termed as prosthetic groups/ co-factors/

co-enzymes. Co-factors bind in transient dissociable

manner either to the enzymes or to the substrate. Most

common co-factors are metal ions. Enzymes that require a

metal ion as co-factor are termed metal activated enzymes.

Prosthetic groups are tightly & stably integrated into a

protein‘s structure by covalent & non covalent forces.

Metals are the main prosthetic groups. Enzymes that

contain tightly bound metal ions or metal ion as prosthetic

group are termed metallo enzymes.

Co-enzymes serve as recyclable shuttles or group transfer

agents that transport many substance from one point

within the substrate from others. B complex group of

vitamins supply important components of numerous co-

enzymes.

ENZYME CLASSIFICATION

1. Oxidoreductasescatalyze oxidations and

reductions, e.g. lactate dehydrogenase

2. Transferases catalyze transfer of groups such as

methyl or glycosyl groups from a donor molecule to an

acceptor molecule, e.g. hexokinase.

3. Hydrolases catalyze the hydrolytic cleavage of C-C,

C-O, C-N, P-O, and certain other bonds, including acid

anhydride bonds, e.g. acetylcholine esterase.

4. Lyases catalyze cleavage of C-C, C-O, C-N, and

other bonds by elimination, leaving double bonds, and

also add groups to double bonds, e.g. aldolase.

5. Isomerases catalyze geometric or structural changes

within a single molecule, e.g. phospho-triose

isomerase.

6. Ligases catalyze the joining together of two

molecules, coupled to the hydrolysis of a

pyrophosphorylgroup in ATP or a similar nucleoside

triphosphate, e.g. acetyl co A carboxylase.

The IUB name of ―hexokinase‖ is ―ATP:D-hexose-6-

phosphotransferaseE.C. 2.7.1.1.‖ This identifies

hexokinase as amember of class 2 (transferases), subclass

7 (transfer of aphosphoryl group), sub-subclass 1 (alcohol

is the phosphorylacceptor). Finally, the term ―hexose-6‖

indicatesthat the alcohol phosphorylated is that of carbon

six ofa hexose.

ACTIVE SITE

Recognition site for binding of substrates. Within active

site, substrates are brought into close proximity to one

another in optimal alignment with the co-factors,

prosthetic groups & amino acids side chains responsible

for catalyzing their chemical transformation into products.

Catalysis is further enhanced by the capacity of active site

to shield substrate from water, & generate an environment

whose polarity, hydrophobicity, acidity or alkalinity can

differ markedly from that of the surrounding cytoplasm.

MODELS FOR ENZYME CATALYSIS

Emil Fischer proposed that specificity with which

enzymes discriminate their substrates when forming an

enzyme substrate complex was analogous to the manner in

which a mechanical lock distinguishes the proper key. The

lock is formed by a cleft or pocket on the protein‘s surface

that forms part of a region called active site.

Lock and key model of enzyme- substrate binding

This model accounted for the exquisite specificity of

enzyme substrate interactions. The implied rigidity of

enzyme‘s active site failed to account for the dynamic

changes that accompany catalysis. This drawback was

addressed by Daniel Khosland‘s induced fit model which

states that when substrate approach & bind to an enzyme,

they induce a conformational change analogous to placing

a hand (substrate) into a glove (enzyme). The enzyme in

turn induces reciprocal changes in its substrates,

harnessing the energy of binding to facilitate the

transformation of substrate into products.

Induced-fit model of enzyme-substrate binding

MECHANISM TO FACILITATE CATALYSIS

Enzymes use various combinations of four general

mechanisms to achieve catalytic enhancement of the rates

of the chemical reaction

Catalysis by proximity

Acid-base catalysis

Catalysis by strain

Covalent catalysis

Enzymes of aspartic protease family (pepsin, lysosomal

cathepsin, HIV protease) illustrate acid-base catalysis.

Serine protease (chymotrypsin) illustrates covalent

catalysis.

Enzymes catalyzing lytic reactions bind their substrates in

a conformation that is unfavorable for the bond that will

undergo cleavage. This conformation mimics that of the

transition state intermediate, a transient specie that

represents the transition state or a half-way point, in the

transformation of substrate into products. In this state

neither free substrate nor product exits. Energy needed to

reach transition state is known as activation energy.

Stabilization of transition state is a general mechanism by

which enzymes accelerate the rates of chemical reactions.

Transition state analogs are more effective enzyme

inhibitors.

ENZYME KINETICS

It is the field of biochemistry concerned with the

quantitative measurement of the rates of enzyme catalyzed

reactions & the systematic study of factors that affect

these rates.

KINETICS OF ENZYME CATALYSIS

Enzymes accelerate the reaction rates by lowering

activation energy needed for the formation of transition

state. The environment of the active site lower activation

energy by stabilizing the transition state intermediate.

Enzymes bind to TSI more tightly than it does to either

substrates or products.

FACTORS AFFECTING THE RATES OF ENZYME

CATALYZED REACTIONS

Multiple factors affect the rate of enzyme catalyzed

reactions.

Temperature- raising the temperature increases the rates

of both un-catalyzed & enzyme catalyzed reactions by

increasing the kinetic energy & the collision frequency of

reacting molecules. Heat energy can also increase the

kinetic energy of the enzyme to a point that exceeds the

energy barrier for disrupting the non-covalent interactions

that maintains its 3-D structure. The polypeptide chain

then begins to unfold or denature with an accompanying

loss of catalytic activity. Enzymes from humans generally

exhibit stability at temperatures upto 45-55C.

Hydrogen ion concentration- most intracellular enzymes

exhibit optimal activity at pH values between 5 & 9.

Relationship of activity to hydrogen ion concentration is

due to enzyme denaturation at high or low pH & effects

on the charged state of the enzymes, substrates, or both.

Substrate concentration- for a typical enzyme, as

substrate concentration is increased Vi increases (due to

more formation of ES complex) until it reaches a

maximum value Vmax. Further increase in substrate

concentration do not further increase Vi (enzyme is

saturated with the substrate). Shape of the curve that

relates substrate concentration to activity is hyperbolic. At

any given instant only substrate molecules that are

combined with the enzyme as an ES complex can be

transformed into a product.

MICHAELIS-MENTEN EQUATION

Michaelis-Menten equation illustrates relationship

between initial reaction velocity Vi& substrate

concentration [S].

Vi = Vmax[S]/KM + [S]

Michaelis-Menten constant (KM), is the substrate

concentration at which the initial velocity is half of the

maximal velocity attainable at a particular concentration

of the enzyme.

LINEAR FORM OF MICHAELIS-MENTEN

EQUATION

The direct measurement of the KM&Vmax often requires

high concentration of substrates to achieve saturating

conditions. A linear form of theMichaelis-Menten

equation circumvents this difficulty & permits Vmax& KM

to be extrapolated from initial velocity data obtained at

less than saturating concentrations of the substrate.

A plot of 1/Vi as a function of 1/ [S], gives a straight line

whose Y intercept is 1/ Vmax& whose slope is KM/ Vmax.

Such a plot is called double reciprocal plot or Line

Weaver Burk plot. X-intercept is -1/ KM , KM is thus

readily calculated from negative x-intercept.

This plot can also be used to determine the kinetic

mechanisms of enzyme inhibitors.

SPECIFIC ACTIVITY, TURN OVER NUMBER,

CATALYTIC CONSTANT

To compare the relative activity of different enzymes or of

different preparations of the same enzyme, several

parameters may be used.

The activity of impure enzyme preparations is expressed

as specific activity (Vmax/ protein concentration).

For a homogeneous enzyme, one may calculate its turn

over number (Vmax/ moles of enzyme present).

If the number of active sites present is known, the

catalytic activity of a homogeneous enzyme is expressed

as its catalytic constantKcat (Vmax/ number of active sites).

Catalytic efficiency of the enzyme is the ratio of two

kinetic constants, Kcat / KM.

ENZYME INHIBITION

Inhibitors of catalytic activities of enzymes can be used

as-

pharmacologic agents

research tools for the study of mechanism of

enzyme action

The strength of interaction between an inhibitor & an

enzyme depends on forces important in protein structure

& ligand binding (hydrogen bonds, electrostatic

interactions, hydrophobic interactions & Van der Waal

forces)

Inhibitors can be classified on the basis of their

site of action on the enzyme

on whether they chemically modify the enzyme

on the kinetic parameter, they influence

Compounds that mimics the transition state of an enzyme-

catalyzed reaction (transition state analogs) or that takes

advantage of the catalytic machinery of an enzyme

(mechanism-based inhibitors) can be potent inhibitors.

Kinetically, we distinguish two classes of inhibitors based

upon whether raising substrate concentration does or does

not overcome the inhibition. Double reciprocal plot

facilitates the evaluation of inhibitors.

COMPETETIVE INHIBITION

Competitive inhibitors resemble substrate (substrate

analog). They bind to the substrate-binding portion of

active site thereby, blocking access by the substrate. Their

effect can be overcome by raising the concentration of

substrate.

Inhibition of the enzyme succinate dehydrogenase by

malonate illustrates competitive inhibition by substrate

analog.Competitive inhibitors act by decreasing the

number of free enzyme molecules available to bind

substrate, i.e. to form ES complex & thus eventually to

form product. A competitive inhibitor has no effect on

Vmax but raises the apparent KM for the substrate.

NON-COMPETETIVE INHIBITION

Anon-competitive inhibitor bear no or little structural

resemblance to the substrate & bind with enzyme at sites

distinct from the substrate binding site. Binding of

inhibitor does not affect the binding of substrate. So,

formation of both EI & EIS complexes is possible. While

E-I complex can still bind the substrate its efficiency at

transforming substrate to product is decreased or generates

product at a negligible rates. Their effects can never be

completely overcome by increase in substrate

concentration. Simple non-competitive inhibitors lower

Vmax but do not affect KM.

IRREVESIBLE INHIBITORS (POISON ENZYMES)

In reversible inhibition the inhibitors form a dissociable

dynamic complex with the enzyme. Fully active enzyme

can be recovered simply by removing the inhibitor from

the surrounding medium. Irreversible inhibitors act

irreversibly by chemically modifying the enzyme. These

modifications generally involve making or breaking

covalent bond with amino acyl residues essential for

substrate binding, catalysis or maintenance of enzyme‘s

functional conformation. These covalent changes are

relatively stable. So, enzyme remains inhibited even after

the removal of the remaining inhibitor from the

surrounding medium e.g. heavy metal atoms, acylating

reagents.

MECHANISM-BASED INHIBITION OR “SUCIDE

INHIBITORS”

Substrate analogs that contain a chemical group that can

be transformed by the catalytic machinery of the target

enzyme. After binding to the active site, catalysis by the

enzyme generates a highly reactive group that forms a

covalent bond & blocks the function of a catalytically

essential residue. They are promising leads for

development of enzyme specific drugs.

FEEDBACK REGULATION

Dietary cholesterol decreases hepatic synthesis of

cholesterol by controlling the expression of the gene that

encodes HMG-Co A reductase (enzyme repression).

FEEDBACK INHIBITION

Feedback inhibition is a process by which the end product

of a multi-step biosynthetic pathway binds to & inhibits an

enzyme catalyzing one of the early step in that pathway.

Feedback inhibitors bear little or no structural similarity to

the substrate of the enzyme they inhibit. They bind at an

allosteric site, spatially distinct from the catalytic site of

the target enzyme. A feedback inhibitors act as negative

allosteric inhibitor & inhibits the first committed step in a

particular biosynthetic sequence. Statins curtail synthesis

of cholesterol by inhibiting HMG-Co A reductase, which

catalyzes a rate limiting state of cholesterol biosynthesis.

In biosynthetic pathways where there are two or more end

products, each end product may only partially inhibit

catalytic activity. The effect of an excess of two or more

end products may be additive or greater than their

individual effect (known as co-operative feedback

inhibition).

PROENZYMES

Proteins that are synthesized & secreted as an inactive

precursor proteins are known as proproteins. Selective or

partial proteolysis converts proprotein to mature protein.

Proproteins forms of enzymes are termed proenzymes or

zymogens. The synthesis & secretion of protease as

proenzyme is to protect the tissue of origin from auto

digestion. E.g. of proproteins include pro-insulin,

pepsinogen, trypsinogen, chymotrypsinogen, several

factors of blood clotting & blood clot dissolution cascade,

& procollagen.

REGULATION OF ENZYME ACTIVITY

Catalytic capacity of the rate-limiting reaction in a

metabolic pathway is the product of concentration of the

enzyme molecules & their intrinsic catalytic efficiency.

Catalytic capacity can be influenced by changing the

quantity of enzyme present & by altering its catalytic

efficiency.

Regulation of enzyme quantity- body proteins are in a

state of dynamic equilibrium, in which they are

continuously synthesized & degraded (turnover). The

absolute quantity of an enzyme is the net balance between

its rate of synthesis & rate of degradation.

Control of enzyme synthesis can be achieved by induction

or repression. Induction of protein synthesis requires hours

to produce significant changes in overall enzyme level.

The ubiquitin-proteasome pathway is responsible both for

the regulated degradation of selected cellular proteins &

for the removal of defective, aberrant proteins. Changes in

protein level generally dominate when meeting long-term

adaptive requirement.

Changes in intrinsic catalytic efficiency can be achieved

by allosteric regulation (binding of dissociable ligands) or

by covalent modification. This can happen within seconds

& best suited for rapid & transient alteration in metabolite

flux.

ALLOSTERIC ENZYMES

Catalysis at the active site may be modulated by the

presence of effectors at an allosteric site. Allosteric sites

are physically distinct from the catalytic sites. They are

multimeric, bind to their substrate at multiple sites (co-

operative binding). Binding of allosteric regulator induces

a conformational change in the enzyme that encompasses

the active site. Shape of the curve that relates changes in

Vi to changes in substrate concentration is sigmoidal,

which is represented by Hill equation.

Two classes of allosterically regulated enzymes are K-

series&V-series. For K-series, the substrate saturation

kinetics is competitive, i.e. KM is raised without an effect

on Vmax. For V-series, the allosteric inhibitors lowers Vmax

without affecting the KM. Alteration in KM or Vmaxare due

to conformational changes at the catalytic site induced by

binding of the allosteric effector at its site. For K-series,

this conformational change may weaken the bonds

between substrate & substrate-binding residues. For V-

series this may be due to alteration in the orientation or

charge of catalytic residues.

ISOZYMES

They are physically distinct versions of a given enzymes,

each of which catalysis the same reaction. Isozymes arise

through gene duplication. They may exhibit differences in

properties such as sensitivity to particular regulatory

factor or substrate affinity that adapt them to specific

tissues or circumstances. Some isozymes may enhance

survival by providing a backup copy of an essential

enzyme. Lactate dehydrogenase is a tetrameric enzyme

consisting of two monomer types- H (for heart) M (for

muscle) that combined to yield five LDH isozymes.

HHHH (I1), HHHM (I2), HHMM (I3), HMMM (I4),

MMMM (I5). Tissue- specific expression of H & M genes

determines the relative proportions of each subunit in

different tissues. Isozyme I1 predominates in heart tissue

& I5 in the liver. Thus, tissue injury releases a

characteristic pattern of LDH isozymes that can be

separated by electrophoresis. Creatine kinase (CK) has

three isozymes CK-MM (skeletal muscle), CK-BB (brain),

& CK-MB (heart & skeletal muscle). CK-MB appears

within 4-6 hours of an MI, peaks at 24 hours & returns to

base line by 48-72 hours. Individual CK isozymes are

separable by electrophoresis, thus facilitating detection.

Reference- Harper‘s Illustrated Biochemistry (29th

edition)

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