References

146

• Aguiyi JC, Guerranti R, Pagani R and Marinello E: Blood chemistry of rats

pretreated with Mucuna pruriens seeds aqueous extracts MP101UJ after Echis

carinatus venom challenge. Phytother res, 15: 712-714, 2001

• Alam MI and Gomes A: Adjuvant effect and antiserum action potentiation by a

(herbal) compound 2-hydroxy-4-methoxy benzoic acid isolated from the root

extract of the Indian medicinal plant ‘Sarsaparilla’ (Hemidesmus indicus).

Toxicon, 36: 1423-1431, 1998

• Anai K, Suzuki M, Yoshida E and Maruyama M: Neutralization of snake venom

hemorrhagic metalloproteinase prevents coagulopathy after subcutaneous

injection of Bothrops jararaca venom in rats. Toxicon, 40: 63-68, 2002

• Anderson SG and Ownby CL: Pathogenesis of hemorrhage induced by proteinase

H from Eastern diamondback rattlesnake (Crotalus adamenteus). Toxicon, 35:

1291–1300, 1977

• Arid SD: Ophidian envenomation strategies and the role of purines. Toxicon, 40:

335-393, 2002

• Arming S, Strobl B, Wechselberger C and Kreil G: In vitro mutagenesis of PH-20

hyaluronidase from human sperm. European journal of Biochemistry, 247: 810-

814, 1997

• Assakura MT, Silva CA, Mentele R, Camargo AC and Serrano SM: Molecular

cloning and expression of structural domains of bothropasin, a P-III

metalloproteinase from the venom of Bothrops jararaca. Toxicon, 41: 217-27,

2003

• Baker JR, Dong S and Pritchard DG: The hyaluronan lyase of Streptococcus

pyogenes bacteriophage H4489A. Biochem J, 365: 317-322, 2002

References

147

• Baramova EN, Shannon JD, Bjarnason JB and Fox JW: Degradation of

extracellular matrix proteins by hemorrhagic metalloproteinases. Arch Biochem

Biophys, 275: 63-71, 1989

• Barkow G, Gutierrez JM and Ovadia M: Inhibition of the hemorrhagic activity of

Bothrops asper venom by a novel neutralizing mixture. Toxicon, 35: 865-877,

1997

• Basavarajappa BS and Gowda TV: Comparative characterization of two toxic

phospholipase A2 from Indian cobra (Naja naja) venom. Toxicon, 30: 1227-1238,

1992

• Beghini DG, da Cruz-Hofling MA, Randazzo-Maura P, Rodrigues-Simioni L,

Novello JC, Hyslop S and Marangoni S: Cross-neutralization of the neurotoxicity

of Crotalus durissus terrificus and Bothrops jararacussu venoms by antisera

against crotoxin and phospholipase A2 from Crotalus durissus cascavella venom.

Toxicon, 46: 604-611, 2005

• Bhaskaran R, Huang CC, Chang DK and Yu C: Cardiotoxin III from Taiwan

cobra (Naja naja atra). Determination of structure in solution and comparison

with short neurotoxins. J Mol Biol, 235: 1291-1301, 1994

• Bhat MK and Gowda TV: Isolation and characterization of a lethal phospholipase

A2 (NN-IVb-PLA2) from the Indian cobra (Naja naja) venom. Biochem Int, 25:

1023-1034, 1991

• Bhat MK and Gowda TV: Purification and characterization of a myotoxic

phospholipase A2 from Indian cobra (Naja naja) venom. Toxicon, 27: 861-873,

1989

References

148

• Bjarnason JB and Fox JW: Characterization of two hemorrhagic zinc proteinases,

toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox)

venom. Biochim Biophys Acta, 911: 356-63, 1987

• Bjarnason JB and Fox JW: Hemorrhagic toxins from snake venoms. Toxin Rev, 7:

121-209, 1988

• Bjarnason JB and Fox JW: Hemorrhagic metalloproteinases from snake venoms.

Pharmac Ther, 62: 325-372, 1994

• Bjarnason JB and Fox JW: Snake venom metallo-endopeptidases: Reprolysins.

Meth Enzymol, 248: part E, pp 345-368 (Barrett, E.J. Ed) New York Academic

press. 1995

• Boman HG and Kaletta U: Chromatography of rattlesnake: A separation of three

phosphodiesterases. Biochim Biophys Acta, 24: 619- 623, 1957

• Bon C and Saliou B: Ceruleotoxin: Identification in the venom of Bungarus

multicinctus, molecular properties and importance of phospholipase A2 activity

for neurotoxicity. Toxicon, 21: 681-698, 1983

• Bon C, Choumet V, Faure G, Jiang MS, Lembezat MP, Radvanyi F and Saliou B:

Biochemical analysis of the mechanism of action of crotoxin, a phospholipase A2

neurotoxin from snake venom. In: Neurotoxins in Neurochemistry, 52, 1988

(Dolly JO, Ed) Chichester: Ellis Horwood.

• Borges MH, Alves DLF, Raslan DS, Pilo-Veloso D, Rodrigues VM, Homsi-

Brandiburgo MI and De Lima ME: Neutralizing properties of Musa paradisica L.

(Musaceae) juice on phosholipase A2, myotoxic, hemorrhagic and lethal activities

of crotalidae venoms. J Ethnopharmacol, 98: 21-29, 2005

References

149

• Borkow G, Gutierrez, JM and Ovadia M: In vitro activity of BaH-1, the main

hemorrhagic toxin of Bothrops asper snake venom on bovine endothelial cells.

Toxicon, 32: 1387–1391, 1995

• Brunda G and Sashidhar RB: Epidemiological profile of snakebite cases from

Andra Pradesh using immunoanalytical approach. Indian J Med Res, 125: 661-

668, 2007

• Bykova LN, Petrov SI and Blagodatskava ZG: Relative acidity of phenol and its

derivatives in a medium of non aqueous solvents. Zh Obshch Khim, 40: 2295-

3000, 1970

• Cevallos MA, Navarro-Duque C, Varela-Julia M and Alagon AC: Molecular mass

determination and assay of venom hyaluronidases by sodium dodecyl sulfate-

polyacrylamide gel electrophoresis. Toxicon, 30: 925–930, 1992

• Chakrabarty D, Bhattacharyya D, Sarkar HS and Lahiri SC: Hemorrhagic protein

of Russell’s viper venom with fibrinolytic and esterolytic activities. Toxicon, 31:

1475-1614, 1993

• Chakrabarty D, Datta K, Gomes A and Bhattacharyya D: Hemorrhagic protein of

Russell’s viper venom with fibrinolytic and esterolytic activities, Toxicon, 38:

1475- 1490, 2000

• Chakrabarty AK, Hall RH and Ghose AC: Purification and characterization of a

potent hemolytic toxin with phospholipase A2 activity from the venom of Indian

Russell’s viper. Mol Cell Biochem, 237, 95-102, 2002

• Chang CC: The action of snake venoms on nerve and muscle. In: Handbook of

Experimental pharmacology, 52: 309-376 (Lee CY., Eds) Berlin: Springer, 1979

References

150

• Chang CC: Neurotoxins with phospholipase A2 activity in snake venoms. Proc

Natnl Sci Counc BROC, 9: 126-142, 1985

• Chang LS, Chen KC, Lin SR and Hung HB: Purification and characterization of

Ophiophagus hannah cytotoxin-like proteins. Toxicon, 48: 429-436, 2006

• Chang WC, Lee ML and Lo TB: Phospholipase A2 activity of long-chain

cardiotoxins in the venom of banded krait (Bungarus fasciatus). Toxicon, 21: 163-

165, 1983

• Chaves F, Barboza M and Gutierrez JM: Pharmacological study of edema induced

by venom of the snake Bothrops asper (terciopelo) in mice. Toxicon, 33: 31-39,

1995

• Chen HS, Tsai HY, Wang YM and Tsai IH: P-III hemorrhagic metalloproteinases

from Russell’s viper venom: Cloning, characterization, phylogenetic and

functional site analyses. Biochimie, 90: 1486- 1498, 2008

• Chen YH, Wang YM, Hseu MJ and Tsai IH: Molecular evolution and structure-

function relationships of crotoxin-like and asparagine-6-containing

phospholipases A2 in pit viper venoms. J Biochem, 381: 25-34, 2004

• Cher CD, Armugam A, Zhu YH and Jeyaseelan K: Molecular basis of

cardiotoxicity upon cobra envenomation. Cell Mol Life Sci, 62: 105-118, 2005

• Chippaux JP, Williams and White J: Snake venom variability: Methods of study

results and interpretations. Toxicon, 29: 1279-1303, 1991

• Chippaux JP: Snakebites: appraisal of the global situation. Bull WHO, 76: 515-

524, 1998

References

151

• Chiu HF, Chen IJ and Teng CHM: Edema formation and degradation of mast

cells by a Phospholipase A2 purified from Trimeresurus mucrosquamatus snake

venom. Toxicon, 27: 115-125, 1989

• Chopra RN, Chopra IC, Handa KL and Kapur LD: In: Chopra’s indigenous drugs

of India, 2nd revised version, Dhar VN and Sons, Kolkata, India, 1958

• Choudhury SR, Gomes A, Gomes A, Dattagupta JK and Sen U: Purification

characterization and preliminary X-ray structural studies of a 7.2 kDa cytotoxin

isolated from the venom of Daboia russellii of the Viperidae family. Acta

Crystallogr Sect F Struct Biol Cryst Commun, 62: 292- 294, 2006

• Chwetzoff S, Tsunasawa S, Sakiyama F and Menez A: Nigexine, a phospholipase

A2 from cobra venom with cytotoxic properties not related to esterase activity.

Purification, amino acid sequence and biological properties. J Biol Chem, 264:

13289-13297, 1989

• Clarke C, Kuruppu S, Reeve S, Ian Smith A and Hodgson WC: Oxylepitoxin-1, a

reversible neurotoxin from the venom of the inland taipan (Oxyuranus

microlepidotus). Peptides, 27: 2655-2660, 2006

• Condrea E, Born, GVR, Farah A, Herken H and Welch AD Ed: Hemolytic effects

of snake venoms. In: Handbook of experimental pharmacology: Springer-verlag,

Berlin, Heidelberg, 448, 1979

• da C B Gouveia AI, da Silveira RB, Nader HB, Dietrich CP, Gremski W and

Veiga SS: Identification and partial characterization of hyaluronidases in

Lonomia obliqua venom. Toxicon, 45: 403-410, 2005

• Daltry JC, Ponnudurai G, Shin CK, Tan NH, Thorpe RS and Wuster W:

Electrophoretic profiles and biological activities: Intraspecific variation in the

References

152

venom of the Malyan pit viper (Colloselasma rhodostoma). Toxicon, 34: 62-79,

1996

• de Faria L, Antunes E, Bon C and de Araujo AL: Pharmacological

characterization of the rat paw edema induced by Bothrops lanceolatus (Fer de

lance) venom. Toxicon, 39: 825-830, 2001

• de Freitas Oliveira C, da Silva Lopes D, Mendes MM, Homsi-Brandeburgo MI,

Hamaguchi A, de Alcantara TM, Clissa PB and de Melo Rodrigues V: Insights of

local tissue damage and regeneration induced by BnSP-7, a myotoxin isolated

from Bothrops (neuwiedi) pauloensis snake venom. Toxicon, article in press, 2009

• Deepa M and Gowda TV: Purification and characterization of a glycoprotein

inhibitor of toxic Phospholipase from Withania somnifera. Arch Biochem

Biophys, 408: 42-50, 2002

• Deoras PJ: Snakes of India. In India the land and the people series, Nationall book

trust, India,1965

• de Souza DH, Selistre- de- Araujo HS, Moura-de- Silva AM, Della- Casa MS,

Oliva G and Garratt RC: Crystallization and preliminary X-ray analysis of

jararhagin, a metalloproteinase/disintegrin from Bothrops jararaca snake venom.

Acta Crystallogr D Biol Crystallogr, 57: 1135-1137, 2001

• Dufton MJ and Hider RC: Conformational properties of the neurotoxins and

cytotoxins isolated from elapid snake venoms. CRC Crit Rev Biochem, 14: 113-

171, 1983

• Engle CM, Becker RR, Bailey T and Bieber AL: Characteristics of two myotoxic

proteins from the venom Crotalus viridis concolor. J Toxic-Toxin Rev, 2: 267-

271, 1983

References

153

• Escalante T, Franceschi A, Rucavado A and Gutierrez JM: Effectiveness of

batimastat, a synthetic inhibitor of matrix metalloproteases in neutralizing local

tissue damge by BaP1, a hemorrhagic metalloproteinase from the venom of the

snake Bothrops asper. Biochem Pharmacol, 60: 269- 274, 2000

• Fazary AE, Taha M and Ju YH: Iron complexation studies of Gallic acid. J Chem

Eng Data, 54: 35- 42, 2009

• Ferrente ND: Turbidometric measurement of acid mucopolysaccharides and

hyaluronidase activity. J Biol Chem, 220: 303-306, 1956

• Fletcher JE and Jiang MS: Possible mechanisms of action of cobra snake venom

cardiotoxins and bee venom melittin. Toxicon, 31: 669-695, 1993

• Fletcher JE, Yang CC and Rosenberg P: Basic phospholipase A2 from Naja

nigricollis snake venom: phospholipid hydrolysis and effects on electrical and

contractile activity of the rat heart. Toxicol Appl Pharmac, 66: 39-54, 1982

• Fox JW and Bjarnason JB: Atrolysins: metalloproteinases from Crotalus atrox

venom. In: Methods in enzymology: protelolytic enzymes: Aspartic and

metallopeptidase, vol 248, pp 345 – 368 (Barrett, A.J., Ed). New York: Academic

press, 1995

• Fox JW and Serrano SM: Structural considerations of the snake venom

metalloproteinases, key members of the M12 reprolysin family of

metalloproteinases. Toxicon, 45: 969-985, 2005

• Franceschi A, Rucavado A, Mora N and Gutiérrez JM: Purification and

characterization of BaH4, a hemorrhagic metalloproteinase from the venom of the

snake Bothrops asper. Toxicon, 38: 63-77, 2000

References

154

• French WJ, Hayes WK, Bush SP, Cardwell MD, Bader JO and Rael ED: Mojave

toxin in venom of Crotalus helleri (Southern Pacific Rattlesnake): molecular and

geographic characterization. Toxicon, 44: 781-91, 2004

• Frost GI, Csoka T and Stern R: The hyaluronidases: a chemical, biological and

clinical overview. Trends in Glycoscience Glycotechnology, 8: 419–434, 1996

• Fry BG: From genome to ‘venome’: molecular origin and evolution of the snake

venom proteome inferred from phylogenetic analysis of toxin sequences and

related bodyproteins. Genome Res, 15: 403-420, 2005

• Futrell J M: Loxoscelism. Am J Med Sci, 304: 261-267, 1992

• Gan SR, Gould RJ, Jacobs JW, Friedman PA and Polokoff MA: Echistatin: A

potent platelet aggregator inhibitor from the venom of the viper Echis carinatus. J

Biol Chem, 26: 19827-19832, 1988

• Gao W, Starkow VG, He ZX, Wang QH, Tsethin VI, Utkin YN, Lin ZJ and Bi

RC: Functions, structures and Triton X-100 effect for the catalytic subunits of

heterodimeric phospholipases A2 from Vipera nikolskii venom. Toxicon, article in

press, 2009

• Ghosh BN, De SS and Chowdhury DK: Separation of the neurotoxin from the

crude venom and study on the action of a number of reducing agents on it. Indian

J Med Res, 29: 367-374, 1941

• Girish KS and Kemparaju K: Inhibition of Naja naja venom hyaluronidase by

plant derived bioactive components and polysaccharides. Biochemistry (Mosco),

70: 1145-1150, 2005

References

155

• Girish KS and Kemparaju K: Inhibition of Naja naja venom hyaluronidase: role

in the management of poisonous bite. Life Sci, 78: 1433-1440, 2006

• Girish KS and Kemparaju K: The magic glue hyaluronan and its eraser

hyaluronidase: A biological overview. Life Sci, 80: 1921-1943, 2007

• Girish KS, Jagadeesha DK, Rajeev KB and Kemparaju K: Snake venom

hyaluronidase: an evidence for isoforms and extracellular matrix degradation. Mol

and Cell Biochem, 240: 105-110, 2002

• Girish KS, Kemparaju K, Nagaraju S and Vishwanath BS: Hyaluronidase

Inhibitors: A biological and therapeutic perspective. Current Medicinal

Chemistry, article in press, 2009

• Girish KS, Mohankumari HP, Nagaraju S, Vishwanath BS and Kemparaju K:

Hyaluronidase and protease activities from Indian snake venoms: Neutralization

by Mimosa Pudica root extract. Fitoterapia, 75: 378-390, 2004(a)

• Girish KS, Shashidhara murthy R, Nagaraju S, Gowda TV and Kemparaju K:

Isolation and characterization of hyaluronidase a “spreading factor” from Indian

cobra (Naja naja) venom. Biochimie, 86: 193–202, 2004(b)

• Giron AA, Stites BG and Gutierrez JM: Antibody-mediated neutralization and

binding-reversal studies on α-neurotoxins from Micrurus nigrocinctus

nigrocinctus (coral snake) venom. Toxicon, 34: 369-380, 1996

• Gmachl M and Kreil G: Bee venom hyaluronidase is homologous to a membrane

protein of mammilian sperm. Proc Natl Acad Sci (USA), 90: 3569-3573, 1993

References

156

• Gomes A, Choudhury SR, Saha A, Mishra R, Giri B, Biswas AK and Debnath A:

A heat stabkle protein toxins (drct-1) from Indian viper (Daboia russelIii) venom

having antiproliferative, cytotoxic and apoptic activities. Toxicon, 49: 45-56, 2007

• Gomes MS, Mendes de Oliveira F, de Andrade RM, Bernardes CP, Hamaguchi

A, de Alcântara TM, Soares AM, Rodrigues VM and Homsi-Brandeburgo MI:

BthMP: A new weakly hemorrhagic metalloproteinase from Bothrops moojeni

snake venom. Toxicon, 53: 24-32, 2009

• Gomis–Ruth FX, Kress LF and Bode W: First structure of a snake venom

metalloproteinase: A prototype for matrix metalloproteinases / collagenases. J Eur

Molec Biol Org, 12: 4151-4157, 1993

• Gong W, Zhu X, Liu S, Teng M and Niu L : Crystal structures of acutolysin A, a

three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of

Agkistrodon acutus, J Mol Biol, 283: 657-68, 1998

• Gopalakrishnakone P, Hawgood BJ, Holbrooke SE, Marsh NA, Santa DE SA S

and Tu AT: Sites of action of Mojave toxin isolated from the venom of the

Mojave rattlesnake. Br J Pharmac, 69: 421-431, 1980

• Gopalakrishnakone P, Ponraj D and Thwin MM: Myotoxic phospholipases from

snake venoms: General myoglobinuric and local myonecrotic toxins. In: Venom

phospholipase A2 enzymes: Structure, Function and Mechanism. Ed by Kini RM.

John Wiley & Sons Ltd. 287-319, 1997

• Gowda TV and Middlebrook JL: Effects of myonecrotic snake venom

phospholipase A2 toxins on cultured muscle cells. Toxicon, 31: 1267-1278, 1993

References

157

• Gowda TV: Interaction of snake venom Phospholipase A2 with plant isolates.

Venom Phospholipase A2 enzymes: Structure, Function and Mechanism (Ed, Kini

RM), John Wiley and Sons Ltd, 1997

• Grotto L, Moroz C, DeVries A and Goldblum N: Isolation of Vipera palestinae

hemorrhagin and distinction between its hemorrhagic and proteolytic activities.

Biochim Biophys Acta, 133: 356–362, 1967

• Gutierrez JM, Arce V, Brenes F and Chaves F: Changes in myofibrillar

components after skeletal muscle necrosis induced by a myotoxin isolated from

the venom of the snakes Bothrops asper. Expt Mol Pathol, 52: 25-37, 1990

• Gutierrez JM and Lomonte B: Phospholipase A2 myotoxins from Bothrops snake

venoms. In: Kini RM (Ed) venom phospholipase A2 enzyme: Structure, Function

and Mechanism. John Wiley and sons. England 321-352, 1997

• Gutierrez JM, Leon G, Rojas G, Lomonte B, Rucavado A and Chaves F:

Neutralization of local tissue damage induced by Bothrops asper (Terciopelo)

snake venom. Toxicon, 36: 1529-1538, 1998

• Gutierrez JM, Romero M, Díaz C and Ovadia M: Isolation and characterization of

a metalloproteinase with weak hemorrhagic activity from the venom of the snake

Bothrops asper (terciopelo). Toxicon, 33: 19-29, 1995

• Gutierrez JM and Rucavado A: Snake venom metalloproteinases: their role in the

pathogenesis of local tissue damage. Biochimie, 82: 841-850, 2000

• Gutiérrez JM, Rucavado A, Chaves F, Díaz C and Escalante T: Experimental

pathology of local tissue damage induced by Bothrops asper snake venom.

Toxicon, article in press, 2009

References

158

• Gutiérrez JM, Rucavado A, Escalante T and Díaz C: Hemorrhage induced by

snake venom metalloproteinases: Biochemical and biophysical mechanisms

involved in microvessel damage. Toxicon, 45: 997-1011, 2005

• Harrison RA, Ibison F, Wilbraham D and Wagstaff SC: Identification of cDNAs

encoding viper venom hyaluronidases: Cross generic sequence conservation of

full length and unusually short variant transcripts. Gene, article in press, 2007

• Harvey AL and Karlsson E: Dendrotoxin from the venom of the green mamba,

Dendroaspis angusticeps. A neurotoxin that enhances acetylcholine release at

neuromuscular junction. Naunyn Schmiedebergs Arch Pharmacol, 312: 1-6, 1980

• Hati AK: Snake bite in west Bengal of India. The snake, 16: 129-130, 1984

• Hawgood B and Bon C: Snake venom presynaptic toxins. Handbook of Natural

Toxins: Reptile and Amphibian venoms, 5: 3-52, 1990

• Heussen C and Dowdle EB: Electrophoretic analysis of plasminogen activators in

polyacrylamide gels containing Sodium dodecyl sulphate and copolymerized

substrates. Anal Biochem, 102: 196-202, 1980

• Hite LA, Jia LG, Bjarnason JB and Fox JW: cDNA sequences for four sanke

venom metalloproteinases: Structure, classification and their relationship to

mammalian reproductive proteins. Arch Biochem Biophys, 308: 182, 1994

• Ho CL and Lee CY: Presynaptic action of Mojave toxin isolated from Mojave

rattlesnake (Crotalus scutulatus) venom. Toxicon, 19: 889-892, 1981

• Ho CL, Ko JL and Lee CY: Differences in pharmacological actions between β-

bungarotoxin and their neurotoxic phospholipases A2 purified from snake venoms.

Proc Natl Sci Counc Repub China, 10: 192, 1986

References

159

• Howes JM, Theakston RDG and Laing GD: Neutralization of the hemorrhagic

activities of viperine snake venoms and venom metalloproteinases using synthetic

peptide inhibitors and chelators. Toxicon, 49: 734- 739, 2007

• Huang KF, Chiou SH, Ko TP, Yuann JM and Wang AH: The 1.35A structure of

cadmium-substituted TM-3, a snake-venom metalloproteinase from Taiwan habu:

elucidation of a TNFalpha-converting enzyme-like active-site structure with a

distorted octahedral geometry of cadmium. Acta Crystallogr D Biol

Crystallor,1118-1128, 2002

• Huang MZ, Wang QC and Liu GF: Effects of an acidic phospholipase A2 purified

from Ophiophagus hannah (king cobra) venom on rat heart. Toxicon, 31: 627-

635, 1993

• Huang Qq, Teng MK and Niu LW: Purification and characterization of two

fibrinogen-clotting enzymes from five-pace snake (Agkistrodon acutus) venom.

Toxicon, 37: 999-1013, 1999

• Huang HC and Lee CY: Isolation and pharmacological properties of

phospholipases A2 from Daboia russellii (Russell’s viper) snake venom. Toxicon,

22: 207-217, 1984

• Igarashi T, Araki S, Mori H and Takeda S: Crystal structures of

catrocollastatin/VAP2B reveal a dynamic, modular architecture of

ADAM/adamalysin/reprolysin family proteins. FEBS Lett, 581: 2416-2422, 2007

• Igarashi T, Oishi Y, Araki S, Mori H and Takeda S: Crystallization and

preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing

proteins (VAPs) from Crotalus atrox venom. Acta Cryst, 62: 688–691, 2006

References

160

• Imai K, Nikai T, Sugihara H and Ownby CL: Hemorrhagic toxin from the venom

of Agkistrodon bilineatus (common cantil). Int J Biochem, 21: 667-673, 1989

• Imato T and Yagishita K: A simple activity measurement of lysozyme. Agric Biol

Chem, 33: 1154-1157, 1971

• Ivanovski G, Petan T, Krizaj I, Gelb MH, Gubensek F and Pungercar J: Basic

amino acid residues in the beta-structure region contribute, but not critically, to

presynaptic neurotoxicity of ammodytoxin A. Biochim Biophys Acta, 1702: 217-

225, 2004

• Iwasaki A, Shieh TC, Shimohigashi Y, Waki M, Kihara H and Ohno M:

Purification and characterization of a coagulant enzyme, Okinaxobin 1, from the

venom of Trimeresurus okinvensis (Himehabu snake) which release

fibrinopeptide B J Biochem, 108: 822-823, 1990

• Izidoro LFM, Rodrigues VM, Rodrigues RS, Ferro EV, Hamaguchi A, Giglio JR

and Homsi-Brandeburgo MI: Neutralization of some hematological and

hemostatic alterations induced by neuwiedase a metalloproteinase isolated from

Bothrops neuwiedi pauloensis snake venom, by the aqueous extract from

Casearia mariquitensis (Flacourtiaceae) Biochimie, 85: 669-675, 2003

• Jagadeesha DK, Shashidhara murthy R, Girish KS and Kemparaju K: A non-toxic

anticoagulant metalloprotease: Purification and characterization from Indian

cobra (Naja naja) venom. Toxicon, 40: 667-675, 2002

• Jang JY, Krishnaswamy T, Kumar T, Gurunathan J, Yang PW and Yu C:

Comparison of the hemolytic activity and solution structures of two snake venom

cardiotoxin analogues which only differ in their N-terminal aminoacid. Biochem,

36: 14635-14641, 1997

References

161

• Januario AH, Santos SL, Marcussi S, Mazzi MV, Pietro RC, Sato DN, Ellena J,

Sampaio SV, Franca SC and Soares AM: Neo-clerodane diterpenoid, a new

metalloproease snake venom inhibitor from Baccharis trimera (Asteraceae): anti-

proteolytic and anti-hemorrhagic properties. Chem Biol Interact, 150: 243- 251,

2004

• Jayanthi GP and Gowda TV: Synergistic interaction of a protease and protease

inhibitors from Russell’s viper (Daboia russellii) venom. Toxicon, 28: 65-74,

1990

• Jedrzejas MJ and Stern R: Structures of vertebrate hyaluronidases and their

unique enzymatic mechanism of hydrolysis. Proteins (Structure Function

Bioinformatics), 61: 227-238, 2005

• Jedrzejas MJ: Pneumococcal virulence factors: Structure and function. Microbiol.

Mol Biol Rev, 65: 187-207, 2001

• Jedrzejas MJ: Structural and functional comparison of polysaccharide-degrading

enzymes. Crit Rev Biochem Mol Biol, 35: 221-251, 2000

• Jia LG, Shimokawa KI, Bjarnason JB and Fox JW: Snake venom

metalloproteinaes: Structure function and relationship to the Adams family of

proteins. Toxicon, 34: 1269, 1996

• Kamiguti AS, Hay CRM, Theakston RDG and Zuzel M: Insights into the

mechanism of hemorrhage caused by snake venom metalloproteinases. Toxicon,

34: 627-642, 1996

References

162

• Kamiguti AS, Theakston RDG, Desmond H and Hutton RA: Systemic

hemorrhage in rats induced by a hemorrhagic fraction from Bothrops jararaca

venom. Toxicon, 29: 1097-1105, 1991

• Kamiguti AS, Zuzel M and Theakston RGD: Snake venom metalloproteinases

and disintegrins: Interactions with cells. Braz J Med Biol Res, 31: 853-862, 1998

• Karlsson E: Chemistry of protein toxins in snake venoms: In: Snake venoms.

Handbook of Experimental pharmacology, 52: 159-212 (Lee CY. ED) Berlin:

Springer, 1979

• Kasturi S and Gowda TV: Purification and characterization of a major

phospholipase A2 from Russell’s viper (Daboia russellii) venom. Toxicon, 27:

229- 237, 1989

• Kasturi S and Gowda TV: Identification, isolation and purification of neurotoxic

phospholipases A2 from Daboia russellii venom using polyclonal antibodies.

Biochem Int, 26: 797- 808, 1992

• Kemeny DM, Dalton N, Lowrence, AJ, Pearce FL and Vernon CA: The

purification and characterization of hyaluronidase from the venom of the honey

bee, Apis mellifera. Eur J Biochem, 139: 217-223, 1984

• Kemparaju K, Krishnakanth TP and Gowda TV: Purification and characterization

of a platelet aggregation inhibitor acidic Phospholipase A2 from Indian saw-scaled

viper (Echis carinatus) venom. Toxicon, 37: 1659-1671, 1999

• Kemparaju K, Prasad BN and Gowda TV: Purification of a basic phospholipase

A2 from Indian saw-scaled viper (Echis carinatus) venom: Characterization of

antigenic, catalytic and pharmacological properties. Toxicon, 32: 1187-1196, 1994

References

163

• Kini RM and Evans HJ: A model to explain the pharmacological effects of snake

venom phospholipase A2. Toxicon, 27: 613-635, 1989

• Kini RM and Evans HJ: Effect of snake venom proteins on blood platelets.

Toxicon, 28: 1387-1422, 1990

• Kini RM and Gowda TV: Studies on snake venom enzymes. Part 11-partal

characterization of ATPase from Russell’s viper (Daboia russellii) venom and

their interaction with potassium. Ind J Biochem Biophysics, 19: 342-346, 1982

• Kini RM, Haar NC and Evans HJ: Non-enzymatic inhibitor of coagulation and

platelet aggregation from Naja nigricollis venom is cardiotoxins. Biochim

Biophys Res Commun, 150: 1012-1016, 1988

• Kini RM, Stefansson S and Evans HJ: Non-Phospholipase anticoagulants from

Naja nigricollis venom: Progress in venom and Toxin research:

(Gopalakrishnakone P and Tan CK, Eds), Singapore, National University of

Singapore,175, 1987

• Kini RM: Proline brackets and identification of potential functional sites in

proteins: Toxins to therapeutics. Toxicon, 36: 1659-1670, 1998

• Kini RM: Structure-function relationships and mechanism of anticoagulant

phospholipase A2 enzymes from snake venoms. Toxicon, 45: 1147-61, 2005

• Kiss G, Zador E, Szalay J, Somagyi J and Ver A: Molecular forms of

acetylcholinesterase in the rat extensor digitorum longus and soleus muscles

regenerating from notexin-induced necrosis. J Muscle Res Cell Motil, 25: 509-

514, 2004

References

164

• Kole L, Chakrabarty D, Datta K, Bhattacharyya D: Purification and

characterization of an organ specific hemorrhagic toxin from Daboia russellii

(Russell’s viper) venom. Indian J Biochem Biophys, 37: 114-120, 2000

• Kondo H, Kondo S, Itezawa H, Murata R and Ohsaka A: Studies on the

quantitative method for determination of hemorrhagic activity of Habu snake

venom. Jap J Med Sci Biol, 13: 43-51, 1960

• Kornalik F and Blomback B: Prothrombin activation induced by Ecarin- a

prothrombin concerting enzyme from Echis carinatus venom. Thromb Res, 6: 53-

63, 1975

• Kostiza T and Meier J: Nerve growth factors from snake venoms: chemical

properties, mode of action and biological significance. Toxicon, 34: 787-806,

1996

• Kreil G: Hyaluronidases-a group of neglected enzymes. Protein Sci, 4: 1666-

1669, 1995

• Kudo K and Tu AT: Characterization of hyaluronidase isolated from Agkistrodon

contortrix contortrix (Southern Copperhead) venom. Arch Biochem Biophys, 386:

154-162, 2001

• Kumar AV and Gowda TV: Novel non-enzymatic toxic peptide of Daboia

russellii (Eastern region) venom renders commercial polyvalent ineffective.

Toxicon, 15: 398- 408, 2006

• Kumar JR, Basavarajappa BS, Arancio O, Aranha I, Gangadhara NS, Yajurvedi

HN and Gowda TV: Isolation and characterization of ‘’Reprotoxin”, a novel

protein complex from Daboia russellii snake venom. Biochimie, 90: 1545- 1559,

2008

References

165

• Kumasaka T, Yamamoto M, Moriyama H, Tanaka N, Sato M, Katsube Y,

Yamakawa Y, Omori-Satoh T, Iwanaga S and Ueki T: Crystal Structure of H2-

proteinase from the venom of Trimeresurus flavoviridis. Biochem, 119: 149-157,

1996

• Laemmli UK: Cleavage of structural proteins during the assembly of the head of

bacteriophage T4. Nature, 227: 680- 685, 1970

• Lakhotia M, Kothari D, Choudhary DR, Sharma S and Jain P: A case of saw-

scaled viper snakebite presenting as Pleuro-pericardial hemorrhage. IACM, 3:

392-394, 2002

• Larsen PR and Wolff J: The toxic proteins of cobra venom. Biochem Pharmacol,

17: 503-510, 1968

• Laurent TC and Fraser JR: Hyaluronan. FASEB J, 6: 2397-2404, 1992

• Laurent TC: The biology of hyaluronan New York: John Wiley & sons,1989

• Lee JY and Spicer AP: Hyaluronan: a multifunctional, megadaton, stealth

molecule. Curr Opin Cell Biol, 12: 581-586, 2000

• Leon G, Estrada R, Chaves F, Rojas G, Ovadia M and Gutierrez JM: Inhibition by

CaNa2EDTA of local tissue damage induced by Bothrops asper (terciopelo)

venom: application in horse immunization for antivenom production. Toxicon, 36:

321-331, 1998

• Leon G, Valverde JM, Rojas G, Lomonte B and Gutierrez JM: Comparative study

on the ability of IgG and Fab sheep anti-venoms to neutralize local hemorrhage,

edema and myonecrosis induced by Bothrops asper (Terciopelo) snake venom.

Toxicon, 38: 233-244, 2000

References

166

• Lewis and Gutmann: Snake venoms and the neuromuscular junction. Semin

Neurol, 24: 175-179, 2004

• Lingott T, Schleberger C, Gutierrez JM and Merfort I: High-resolution crystal

structure of the snake venom metalloproteinase BaP1 complexed with a

peptidomimetic: insight into inhibitor binding. Biochem, 48: 6166-6174, 2009

• Liu Z, Li W, Zang H, Han Y and Lai L: Modeling the third loop of short-chain

snake venom neurotoxins: Roles of the short-range and long-range interactions.

Protein: Structure Function and Genetics, 42: 6-16, 2001

• Lomonte B and Gutierrez JM: A new muscle damaging toxin, myotoxin II. From

the venom of the snake Bothrops asper (terciopelo). Toxicon, 27: 725-733, 1989

• Lomonte B, Leon G and Hanson LA: Similar effectiveness of Fab and F (ab)2

anti-venoms in the neutralization of hemorrhagic activity of Vipera berus snake

venom in mice. Toxicon, 34: 1197-1202, 1996

• Lomonte B, Lundgren J, Johansson B and Bagge U: The dynamics of local tissue

damage induced by Bothrops asper snake venom and myotoxin II on the mouse

Cremaster muscle: an intravital and electron microscopic study. Toxicon, 32: 41-

55, 1994

• Lomonte B, Tarkowski A and Hanson HA: Host response to Bothorpas asper

snake venom: analysis of edema formation, inflammatory cells and cytokine

release in a mouse model. Inflammation, 18: 93-105, 1993

• Lowry OH, Rosebrough NJ, Farr AL and Randall RJ: Protein measurement with

Folin phenol reagent. J Biol Chem, 193: 265-275, 1951

References

167

• Lu G, Kochoumian and King TP: Sequence identity and antigenic cross reactivity

of white face hornet venom allergen, also a hyaluronidase, with other proteins. J

Biol Chem, 270: 4457-4465, 1995

• Lumsden NG, Banerjee Y, Kini RM, Kuruppu S and Hodgson WC: Isolation and

characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom

of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake).

Neuropharmaco, 52: 1065-1070, 2007

• Maeda N, Tamiya N, Pattabhiraman TR and Russell FE: Some chemical

properties of the venom of the rattlesnake Crotalus viridis helleri. Toxicon, 16:

431-441, 1978

• Mahanta M and Mukherjee AK: Neutralization of lethality, myotoxicity and toxic

enzymes of Naja kaouthia venom by Mimosa pudica root extracts. J

Ethnopharmacol, 75: 55-60, 2001

• Maity G, Mandal S, Chatterjee A and Bhattacharyya D: Purification and

characterization of a low molecular weight multifunctional cytotoxic

phospholipase A2 from Russell’s viper venom. J Chromatogr B Analyt Technol

Biomed Life Sci, 845: 232- 243, 2007

• Mandal S and Bhattacharyya D: Two L-amino oxidase isoenzymes from Russell’s

viper (Daboia russellii) venom with different mechanisms of inhibition by

substrate analogs. FEBS, 275: 2078- 2095, 2008

• Mandelbaum AP and Assakura MT: Isolation and characterization of a proteolytic

enzyme from the venom of the snake Bothrops jararaca (Jararaca). Toxicon, 20:

955-972, 1982

References

168

• Marcussi S, Bernardes CP, Santos-Filho NA, Mazzi MV, Oliveira CZ, Izidoro

LF, Fuly AL, Magro AJ, Braz AS, Fontes MR, Giglio JR and Soares AM:

Molecular and functional characterization of a new non-hemorrhagic

metalloprotease from Bothrops jararacussu snake venom with anti platelet

activity. Peptide, 28: 2328-2339, 2007

• Markland FS: Snake venom and haemostatic systems. Toxicon, 36: 1749-1800,

1998

• Markovic-Housley Z, Miglierini G, Soldatova L, Rizkallah PJ, Muller U and

Schirmer T: Crystal structure of hyaluronidase, a major allergen of bee venom.

Structure, 8: 1025–1035, 2000

• Martz W: Plants with a reputation against snakebite. Toxicon, 30: 1131-1142,

1992

• Maruyama M, Sugiki M, Yoshida E, Shimaya K and Mihara H: Broad substrate

specificity of snake venom fibrinolytic enzymes: possible role in hemorrhage.

Toxicon, 30: 1387-1397, 1992

• Matsue T, Fujimura Y and Titani K: Snake venom proteases affecting hemostasis

and thrombosis. Biochim Biophys Acta, 1477: 146-156, 2000

• Maung-Maung-Thawin P, Gopalkrishnakone R, Yuen CH and Tan: A major

lethal factor of venom of Burmese Russell’s viper (Doboia russellii siamensis),

Isolation, N-terminal sequences of biological activities of daboiatoxin. Toxicon,

33: 3-76, 1995

• Mazzi MV, Marcussi S, Carlos GB, Stábeli RG, Franco JJ, Ticli FK, Cintra AC,

França SC, Soares AM and Sampaio SV: A new hemorrhagic metalloprotease

References

169

from Bothrops jararacussu snake venom: Isolation and biochemical

characterization. Toxicon, 44: 215-23, 2004

• Mebs D and Samejima Y: Isolation and characterization of myotoxic

Phospholipase A2 from crotalid venoms. Toxicon, 24: 161-168, 1986

• Mebs D: Myotoxic activity of Phospholipase A2 isolated from cobra venom:

neutralization by polyvalent anti-venoms. Toxicon, 24: 1001-1008, 1986

• Meier J and Theakston RDG: Approximate LD50 determination of snake venoms

using eight to ten experimental animals. Toxicon, 24: 395-401, 1986

• Menez A: Functional architectures of animal toxins: A clue to drug design?

Toxicon, 36: 1557-1572, 1998

• Menzel EJ and Farr C: Hyaluronidase and its substrate hyaluronan: biochemistry,

biological activities and therapeutic uses. Cancer Lett, 131: 3-11, 1998

• Meyer K: Hyaluronidases In: Enzymes: (Boyer PD, Ed), New York; Academic

Press, 307-320, 1971

• Mir R, Sinha M, Sharma S, Sinngh N, Kaur P, Srinivasan A and Singh TP:

Isolation, purification, crystallization and preliminary crystallographic studies of

sagitoxin, an oligomeric cardiotoxin from the venom of Naja saggitifera. Acta

Crystallogr Sect F Struct Biol Cryst Commun, 64: 545-547, 2008

• Mirtschin PJ: Fatal cerebral hemorrhage after snakebite (letter; comment). Med J

Aust, 155: 850-851, 1991

References

170

• Mors WB, Nascimento MC, Pereira BMR and Pereira NA: Plant natural products

active against snakebite and the molecular approach. Phytochem, 55: 627-642,

2000

• Moura-da-Silva AM, Della-Casa MS, David AS, Assakura MT, Butera D, Lebrun

I, Shannon JD, Serrano SMT and Fox JW: Evidence for heterogeneous forms of

the snake venom metalloproteinase jararahagin: a factor contributing to snake

venom variability. Arch Biochem Biophys, 409: 395-401, 2003

• Mukherjee AK: Characterization of a novel pro-coagulant metalloprotease

(RVBCMP) processing alpha-fibrinogenase and tissue hemorrhagic activity from

venom of Daboia russellii (Russell’s viper): evidence of distinct coagulant and

hemorrhagic sites in RVBCMP. Toxicon, 51: 923- 933, 2008

• Muniz MR, Ambrosio AL, Selistre-de-Araujo HS, Cominetti MR, Moura-da-

Silva AM, Oliva G, Garratt RC and Souza DH: The three-dimensional structure of

bothropasin, the main hemorrhagic factor from Bothrops jararaca venom:

insights for a new classification of snake venom metalloprotease subgroups.

Toxicon, 52: 807-816, 2008

• Murakami MT, Lourenzoni MR, Arruda EZ, Tomaz MA, Vicoti MM, Abrego JR,

Melo PA and Arni RK: Biochemical and structural investigations of

Bothropstoxin-II, a myotoxic Asp49 phospholipase A2 from Bothrops jararacussu

venom: Protein Pept Lett, 15: 1002-1008, 2008

• Nadkarni AK: In: Dr. Nadkarni’s Indian Materia Medica. 3rd revised enlarged

edition, 2: Popular prakashan, Bombay: India, 1976

• Nagaraju S, Mahadeshwaraswamy YH, Girish KS and Kemparaju K: Venom

from spiders of the genus Hippasa: Biochemical and pharmacological studies.

Comp Biochem Physiol, 144: 1-9, 2006

References

171

• Neto HS and Marques MJ: Microvessel damage by Bothropus jararacussu snake

venom: pathogenesis and influence on muscle regeneration. Toxicon, 46: 814-819,

2005

• Ng HC, Ranganathan S, Chua KL and Khoo HE: Cloning and molecular

characterization of the first aquatic hyaluronidase, SFHYA1, from the venom of

stonefish (Synanceja horrida). Gene, 346: 71-81, 2005

• Nirthanan S, Gao R, Gopalkrishnakone P, Gwee MCF, Khoo HE, Cheah LS and

Kini RM: Pharmacological characterization of mitatoxin, an α-neurotoxin isolated

from the venom of the New-Guinean small-eyed snake Micropechis ikaheta.

Toxicon, 40: 863-871, 2002

• Nolan C, Hall LS and Barlow GH: Ancord, the coagulating enzyme from

Malayan pit viper (Agkistrodon rhodostoma) venom. Methods Enzymol, 45: 205,

1976

• Obrig TG, Louise CB, Moran TP, Mori N and Tu AT: Direct cytotoxic effects of

hemorrhagic toxins from Crotalus ruber ruber and Crotalus atrox on human

vascular endothelial cells, in vitro. Microvasc Res, 46: 412-416, 1993

• Oda T, Ohta M, Inoue S, Ikeda K, Furukawa S and Hayashi K: Amino acid

sequence of nerve growth factor purified from the venom of the Formosan cobra

Naja atra. Biochem Int, 19: 909-917, 1989

• Ohsaka A: Hemorrhagic, necrotizing and edema forming effects of snake venoms.

In: Snake venoms. Handbook of Experimental Pharmacology, 52: 480, (Lee CY,

Ed), Berlin; Springer-verlag, 1979

• Oliveira CZ, Maiorano VA, Marcussi S, Sant’ Ana CD, Januario AH, Lourenco

MV, Sampaio SV, Franca SC, Pereira PA and Soares AM: Anticoagulant and

References

172

antifibrinogenolytic properties of the aqueous extract from the Bauhinia forficate

against snake venoms. J Ethnopharmacol, 98: 213-216, 2005

• Ondetti MA, Williams NJ, Sabo EF, Pluscec J, Weaver ER and Kocy O:

Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca.

Isolation, elucidation of structure and synthesis. Biochem, 10: 4033-4039, 1971

• Ouyang C and Teng CM: Fibrinogenolytic enzymes of Trimeresurus

mucrosquamatus venom. Biochimica Biophysica Acta, 420: 298-308, 1976

• Ouyang C, Teng CM and Huang TF: Characterization of snake venom

components acting on blood coagulation and platelet function. Toxicon, 30: 945-

966, 1992

• Ouyang CH, Ma YH, Jih HC and Teng CM: Characterization of the platelet

aggregation inducer and inhibitor from Echis carinatus snake venom. Biochemica

Biophysica Acta, 841: 1-7, 1985

• Ownby CL, Cameron D and Tu AT: Isolation of myotoxic component from

rattlesnake (Crotalus viridis viridis) venom. Electron microscopic analysis of

muscle damage. Am J Pathol, 85: 149-166, 1976

• Ownby CL, Nika T, Imai K and Sugihara H: Pathogenesis of hemorrhage induced

by bilitoxin, a hemorrhage toxin isolated from the venom of the common cantil

(Agkistrodon bilineatus bilineatus). Toxicon, 28: 837-846, 1990

• Ownby CL: Pathology of rattlesnake envenomation. In: Rattlesnake venoms:

Their Actions and Treatment, 163-209 (Tu, AT., Ed), New York: Marcel Dekker.

1982

• Paul VK: Animal and insect bites. In: Singh M (Ed). Medical Emergencies in

Children, 2nd Ed, New Deihi, Sagar Publications, 1993

References

173

• Peng M, Lu W, Beviglia L, Niewiarowski S, Kirby EP and Echicetin: A Snake

venom protein that inhibits binding of von willebrand factor and alboaggregins to

platelets glycoprotein lb. Blood, 81: 2321-2328, 1993

• Pessini AC, Takao TT, Cavalheiro EC, Vichnewski W, Sampaio SV, Giglio JR

and Arantes EC: A hyaluronidase from Tityus serrulatus scorpion venom:

isolation, characterization and inhibition by flavonoids. Toxicon, 39: 1495-1504,

2001

• Petretski JH, Kanashiro MM, Rodrigues FR, Alves EW, Machado OL and Kipnis

TL: Edema induction by the disintegrin-like/cysteine-rich domains from a

Bothrops atrox hemorrhagin. Biochem Biophys Res Commun, 276: 1629-1634,

2000

• Philip E: Snakebite and Scorpian sting. Chapter 28 In: Pediatric and Neonatal

Emergency care. (Srivatava RN, Ed): 227-234, 1994

• Poh CH, Yuen R, Chung MC and Khoo HE: Purification and partial

characterization of hyaluronidase from Stone fish (Synanceja horrida) venom.

Comp Biochem Physiol, 101: 159-163, 1992

• Poulsen TT, Pedersen N, Perin MS, Hansen CK and Poulsen HS: Specific

sensitivity of small cell lung cancer cell lines to the snake venom toxin taipoxin.

Lung Cancer, 50: 329-337, 2005

• Prasad BN, Kemparaju K, Bhatt KG and Gowda TV: A platelet aggregation

inhibitor phospholipase A2 from Russell’s viper (Daboia russellii) venom:

isolation and characterization. Toxicon, 34:1173-1185, 1996

• Punde DP: Management of snakebite in rural Maharashtra: a 10 year experience.

Nat Med J India, 18: 71-75, 2005

References

174

• Quick AJ: The prothrombin in haemophilia and obstructive jaundice. J Biol

Chem, 107: 73-85, 1935

• Radis-Baptista G, Oguiura N, Hayashi MAF, Camargo ME, Grego KF, Oliveira

EB and Yamane T: Nucleotide sequence of crotamine isoform precursors from a

single South American Rattlesnake (Crotalus durissus terificus). Toxicon, 37:

973-984, 1999

• Ramanaiah M, Parthasarathy PR and Venkaiah B: Isolation and characterization

of hyaluronidase from scorpion (Heterometrus fulvipes) venom. Biochem Int, 20:

301-310, 1990

• Ramos OHP and Selistre-de-Araujo HS: Snake venom metalloproteases-structure

and function of catalytic and disintegrin domains. Comp Biochem Physiol, 142:

328-346, 2006

• Rash LD and Hodgson WC: Pharmacology and biochemistry of spider venoms.

Toxicon, 40: 225-254, 2002

• Reid HA and Thekaston RDG: The management of snakebites. Bull WHO, 63:

885-895, 1983

• Reid HA: Venomous bites and stings. In: Black JA, Ed. Paediatric Emergencies.

London; Butterworths, 1979

• Reissig JL, Stominger JL and Lolir LF: A modified colorimetric method for the

estimation of N-acetylamino sugars. J Biol Chem, 217: 959-966, 1955

• Rigden DJ, Jedrzejas MJ and deMello LV: Identification and analysis of catalytic

TIM barrel domains in seven further glycoside hydrolase families. FEBS Letters,

544: 103-111, 2003

References

175

• Rodrigus RS, Izidoro LF, Teixeira SS, Silveira LB, Hamaguchi A, Homsi-

Brandeburgo MI, Selistre-de-Araujo HS, Giglio JR, Fuly AL, Soares AM and

Rodrigues VM: Isolation and functional characterization of a new myotoxic acidic

phospholipase A2 from Bothrops pauloensis snake venom. Toxicon, 50: 153-165,

2007

• Rong H, Li Y, Lou XH, Zhang X, Gao YX, Teng MK and Niu LW: Purification,

partial characterization, crystallization and preliminary X-ray diffraction of a

novel cardiotoxin-like basic protein from Naja naja atra (South Anhui) venom.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 63: 130-134, 2007

• Rosenberg P, Condrea E, Rapvano BE, Soons KR and Yang CC: Dissociation of

pharmacological and enzymatic activities of snake venom phospholipase A2 by

modication of corboxylate groups. Biochem Pharmacol, 32: 3525-3530, 1983

• Rossetto O and Montecucco C: Presynaptic neurotoxins with enzymatic activities.

Handb Exp Pharmacol, 184: 129-170, 2008

• Rossetto O, Rigoni M and Montecucco C: Different mechanism of blockade of

neuroexocytosis by presynaptic neurotoxins. Toxicol Lett, 149: 91-101, 2004

• Rothschild AM and Rothschild Z: Liberation of pharmacologically active

substances by snake venoms. In: Lee CY (Eds), Handbook of Experimental

pharmacology, 52, Snake venoms. Springer-Berlin, 591-625, 1979

• Rucavado A, Escalante T, Franceschi A, Chaves F, Leon G, Curry Y and Ovadia

M: Inhibition of local hemorrhage and dermonecrosis induced Bothropus asper

snake venom: effectiveness of early in situ administration of the peptidomimetic

References

176

metalloprotease inhibitor batimastat and the chelating agent CaNa2EDTA. Am J

Trop Med Hyg, 63: 313-319, 2000

• Rucavado A and Lomonte B: Neutralization of myonecrosis, hemorrhage and

edema induced by Bothrops asper snake venom by homologous and heterologous

pre-existing antibodies in mice. Toxicon, 34: 567-578, 1996

• Rucavado A, Henríquez M, García J and Gutiérrez JM: Assessment of

metalloproteinase inhibitors clodronate and doxycycline in the neutralization of

hemorrhage and coagulopathy induced by Bothrops asper snake venom. Toxicon,

52: 754-759, 2008

• Rudrammaji LMS: Characterization of phospholipase A2 inhibitor from Indian

cobra (Naja naja) venom. Ph.D. thesis submitted to University of Mysore,

Mysore, India, 1994

• Russel FE and Brodie AF: In: Chemical Zoology (Florkin M and Scheer BT, Ed.),

IX Amphibia and Reptilia, 449, Academic press, New York, London, 1974

• Russell FE: Snake venom poisoning. JB. Lipincott: Philadelphia, Toronto, 1980

• Saitoh H, Takagaki K, Majima M, Nakamura T, Matsuki A, Kasai M, Narita H

and Endo M: Enzymatic reconstruction of glycosaminoglycan oligosaccharide

chains using the transglycosylation reaction of bovine testicular hyaluronidase. J

Biol Chem, 270: 3741-3747, 1995

• Salvini TF, Amaral AC, Miyabara EH, Turri JAO, Danella PM and Selistre de

Araujo HS: Systemic skeletal muscle necrosis induced by crotoxin. Toxicon, 39:

1141-1149, 2001

References

177

• Samel M, Subbi J, Siigur J and Siigur E: Biochemical characterization of

fibrinogenolytic serine proteases from Vipera labetina snake venom. Toxicon, 40:

51-54, 2002

• Samson AO, Chill JH and Anglister J: Two-dimensional measurement of proton

T1rho relaxation in unlabeled proteins: mobility changes in alpha-bungarotoxin

upon binding of an acetylcholine receptor peptide. Biochem, 44: 10926-10934,

2005

• Sanchez EE, Rodríguez Acosta A, Palomar R, Lucena SE, Bashir S, Soto JG and

Pérez JC: Colombistatin: a disintegrin isolated from the venom of the South

American snake (Bothrops colombiensis) that effectively inhibits platelet

aggregation and SK-Mel-28 cell adhesion. Arch Toxicol, 83: 271-279, 2009

• Sasa M: Diet and snake venom variation: Can local selection alone explain

intraspecific venom variation. Toxicon, 37: 249-252, 1999

• Satake M, Murata Y and Suzuki T: Studies on snake venoms XIII.

Chromatographic separation and properties of three proteinases from Agkistrodon

halys blomhoffii venom. J Biochem, 53: 483– 497, 1963

• Sathyavati GV, Raina MK and Sharma M: In: Medicinal plants of India. ICMR,

New Delhi, India, 1976

• Satish S, Tejaswini J, Krishnakantha TP and Veerabasappa Gowda T: Purification

of a Class B1 platelet aggregation inhibitor phospholipase A2 from Indian cobra

(Naja naja) venom. Biochimie, 86: 203-210, 2004

References

178

• Sato S, Yoshida H, Abe H and Tamiya N: Properties and biosynthesis of a

neurotoxic protein of the venoms of sea snakes Laticauda laticauda and

Laticauda colubrina. Biochem J, 115: 85-90, 1969

• Schffman S, Threodor I and Rapaport: Separation from Russell’s viper venom of

one factor reaching with factor X and another reaching with factor V. Biochem, 8:

1397-1405, 1969

• Schiavavo G, Matteoli M and Montecucco C: Neurotoxins affecting

neuroexocytosis. Physiol Rev, 80: 717-766, 2000

• Serrano SM, Wang D, Shannon JD, Pinto AF, Polanowska-Grabowska RK and

Fox JW: Interaction of the cysteine-rich domain of snake venom

metalloproteinases with the A1 domain of von Willebrand factor promotes site-

specific proteolysis of von Willebrand factor and inhibition of von Willebrand

factor-mediated platelet aggregation. FEBS J, 274: 3611-3621, 2007

• Shannon JD, Baramova EN, Bjarnason JB and Fox JW: Amino acid sequence of a

Crotalus atrox venom metalloproteinase which cleaves type IV collagen and

gelatin. J biol Chem, 264: 11575-11583, 1989

• Shashidhara murthy R, Jagadeesha DK, Girish KS and Kemparaju K: Variation in

biochemical and pharmacological properties of Indian cobra (Naja naja) venom

due to geographical distribution. Mol Cell Biochem, 229: 93-101, 2002

• Shelke RR, Satish S and Gowda TV: Isolation and characterization of a novel

postsynaptic/cytotoxic neurotoxin from Daboia russellii venom. J Pep Res, 59:

257-263, 2002

References

179

• Shimizu MT, Jorge AOC, Unterkircher CS, Fantinato V and Paula CR: J Med Vet

Mycol, 33: 27-31, 1995

• Siigur J and Siigur E: Polypeptides and proteins active in coagulation process:

Methods and Tools in Biosciences and Medicine (Animal Toxins, Ed. by Rochat

H, Martin-Eauclaire M-F), 2000

• Slotta KH and Fraenkel-Conrat H: Two active proteins from rattlesnake. Nature,

142: 213-218, 1938

• Soares AM, Ticli FK and Marcussi S: Medicinal plants with inhibitory properties

against snake venoms. Curr Med Chem, 12: 2625-2641, 2005

• Spicer and McDonald: Characterization and molecular evolution of a vertebrate

hyaluronan synthase gene family. J Biol Chem, 273: 1923–1932, 1998

• Stern R and Jedrzejas MJ: Hyaluronidases: Their genomics, structures and

mechanisums of action. Chem Rev, 106: 818-839, 2006

• Stocker KF and Barlow GH: The coagulant enzyme from Bothrops atrox venom

(Batroxobin). Methods Enzymol, 45: 214, 1976

• Storella RJ, Schouchoff AL, Fuji M, Hill J, Fletcher JE, Jiang MS and Smith LA:

Preliminary evidence for a postsynaptic action of β-bungarotoxin in mammalian

skeletal muscle. Toxicon, 30: 349-354, 1992

• Stroka A, Donato JL, Bon C, Hyslop S and de Araújo AL: Purification and

characterization of a hemorrhagic metalloproteinase from Bothrops lanceolatus

(Fer-de-lance) snake venom. Toxicon, 45: 411-420, 2005

References

180

• Takeda S, Igarashi T and Mori H: Crystal structure of RVV-X: an example of

evolutionary gain of specificity by ADAM proteinases. FEBS Lett, 581: 5859-

5864, 2007

• Tan LC, Kuruppu S, Smith A, Reeve S and Hodgson WC: Isolation and

pharmacological characterization of hostoxin-1, a postsynaptic neurotoxin from

the venom of the Stephen's banded snake (Hoplocephalus stephensi).

Neuropharmaco, 51: 782-788, 2006

• Teng CM, Ouyang C and Lin SC: Species difference in the fibrinogenolytic

effects of α and β-fibrinogenases from Trimeresurus mucrosquamatus snake

venom. Toxicon, 23: 777-782, 1985

• Teng CM, Wang JP, Peng HC and Ouyang C: Edema-producing protein isolated

from Trimeresurus mucrosquamatus snake venom. Toxicon, 27: 899-905, 1989

• Theakston RDG and Warrell DA: Antivenoms: A list of hyperimmune sera

currently available for the treatment of envenoming by bites and stings. Toxicon,

29: 1419-1470, 1991

• Tsai IH, Tsai HY, Wang YM, Tun-Pe and Warrell DA: Venom phospholipases of

Russell’s vipers from Myanmar and eastern India- Cloning, characterization and

phylogeographic analysis. Biochem Biophys Acta, 1774: 1020-1028, 2007

• Trebien HA and Calixo JB: Pharmacological evaluation of rat paws edema

induced by Bothrops Jararaca venom. Agents Actions, 26: 292-300, 1989

• Tu AT and Hendon RR: Characterization of lizard venom hyaluronidase and

evidence for its action as a spreading factor. Comp Biochem Physiol, 76: 337-383,

1983

References

181

• Tu AT: Tissue damaging effects by snake venoms: hemorrhage and myonecrosis.

In: Tu AT (Ed,)5: Handbook of Natural Toxins, 297-347, 1991

• Tzeng MC, Hseu MJ, Yang JH and Guillory RJ: Specific binding of three

neurotoxins with phospholipase A2 activity to synaptosomal membrane

preparations from the Guinea pig brain. J Protein Chem, 5: 221-228, 1986

• Ushanandini S, Nagaraju S, Harish Kumar K, Vedavathi M, Machiah DK,

Kemparaju K, Vishwanath BS, Gowda TV and Girish KS: The anti-snake venom

properties of Tamarindus indica (leguminosae) seed extract. Phytother Res, 20:

851-858, 2006

• Ushanandini S, Nagaraju S, Nayaka SC, Kumar KH, Kemparaju K and Girish KS:

The anti-ophidian properties of Anacardium occidentale bark extract.

Immunopharmacol Immunotoxicol, article in press, 2009

• Ushanandini S: Isolation and characterization of hemorrhagic complexes in

eastern regional Russell’s viper (Daboia russellii) venom. Ph.D., thesis submitted

to University of Mysore, Mysore, India, 2006

• Venyaminov SY and Yang JT: In Circular dichroism and the conformational

analysis of biomolecules; G.D. Fasman, Ed.; Pelenum Press, Ney York, pp.

69,1996

• Viljoen CC, Botes DP and Kruger H: Isolation and amino acid sequence of

caudoxin, a presynaptic acting toxic phospholipase A2 from the venom of the

horned puff adder (Bitis caudalis). Toxicon, 20: 715-737, 1982

• Vishwanath BS and Gowda TV: Interaction of aristolochic acid with Daboia

russellii phospholipase A2: Its effect on enzymatic and pathological activities.

Toxicon, 25: 929-937, 1987

References

182

• Vishwanath BS, Kini RM and Gowda TV: Characterization of three edema

inducing Phospholipase A2 enzymes from habu (Trimeresurus flavoviridis)

venom and their interaction with the alkaloid aristolochic acid. Toxicon, 25: 501-

515, 1987

• Wang WJ, Shih CH and Huang TF: Primary structure and antiplatelet mechanism

of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom.

Biochimie, 87: 1065-77, 2005

• Wang Z, Zhuang M, Shu Y, Zhang H, Song S and Lin Z: Crystallization and

preliminary X-ray analysis of cardiotoxic phospholipase A2 from Ophiophagus

hannah (king cobra). Acta Crystallogr D Biol Crystallogr, 57: 709-710, 2001

• Warrell DA: Clinical features of envenoming from snake bites. Envenoming and

their treatments. (In: Bon, C. Goyffon M, Ed), Foundation Marcel Merieux, Lyon,

pp. 63-76, 1996

• Warrell DA: Tropical snakebite: clinical studies in South East Asia in: Natural

toxins-animal, plant and microbial, (Harris, J.B. Ed) Clarendon press Oxford, 25,

1986

• Watanabe L, Shannon JD, Valente RH, Rucavado A, Alape-Girón A, Kamiguti

AS, Theakston RD, Fox JW, Gutiérrez JM and Arni RK: Amino acid sequence

and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake

venom that exerts multiple tissue-damaging activities. Protein Sci, 12: 2273-2281,

2003

• Weiland H and Konz W: Einige Beobachtugen am eift der Brillenschlangen (Naja

tripudians). Sitzungber, Bayerische Akad Wiss Math Naturwiss Abteil, 177: 1936

• Weltzien HU: Cytolytic and membrane-perturbing properties of

lsophosphatidylcholine. Biochim Biophys Acta, 559: 259-287, 1979

References

183

• Westerlund B, Nordlund P, Uhlin U, Eaker D and Eklund H: The three-

dimensional structure of notexin, a presynaptic neurotoxic phospholipase A2 at

2.0 A resolution. FEBS Lett, 301: 159-164, 1992

• Whitaker R and Captain A: A field guide to snakes of India, 2004

• Williams C, do Nascimento, Amarasiriwardana D and Xing B: Comparison of

natural organic acids and synthetic chelates at enhancing phyto extraction of

metals from a multi-metal contaminated soil. Environ Pollut, 140: 114-123, 2006

• Wilson HI, Nicholson GM, Tyler MI and Howden ME: Induction of giant

miniature end-plate potentials during blockade of neuromuscular transmission by

textilotoxin. Naunyn Schmiedebergs Arch Pharmacol, 352: 79-87, 1995

• Wuster W and Harvay AL: Reviews of venomous snake systematic in toxicon.

Toxicon, 34: 397-398, 1996

• Wuster W, Golay P and Warrell DA: Synopsis of recent developments in

venomous snake systematic. Toxicon, 35: 319-340, 1997

• Wuster W: The genus Daboia (Serpentes: Viperidae): Russell’s viper,

Hamadryad, 23: 33-40, 1998

• Xu X, Wang X, Xi X, Liu J, Huang J and Lu Z: Purification and partial

characterization of hyaluronidase from five pace snake (Agkistrodon acutus)

venom. Toxicon, 20: 973-981, 1982

References

184

• Yamaguchi Y, Shimohigashi Y, Chijiwa T, Nakai M, Ogawa T, Hattori S and

Ohno M: Characterization, amino acid sequence and evolution of edema inducing,

basic Phospholipase A2 from Trimeresurus flavoviridis venom. Toxicon, 39:

1069-1076, 2001

• Yang CC and Chang LS: Biochemistry and molecular biology of snake

neurotoxin. J Chin Chem Soc, 46: 319-333, 1999

• Yingprasertchai S, Bunyasrisawt S and Ratanabanangkoon K: Hyaluronidase

inhibitors (sodium cromoglycate and sodium auro-thiomalate) reduce the local

tissue damage and prolong the survival time of mice injected with Naja kaouthia

and Calloselasma rhodostoma venoms. Toxicon, 42: 635-646, 2003

• Zhang D, Botos I, Gomis–Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode

W and Meyer E: Structural interaction of natural and synthetic inhibitors with the

venom metalloproteinase, atrolysin C (Ht-d). Proc Natn Acad Sci, 91: 8447, 1994

• Zhu X, Teng M and Niu L: Structure of acutolysin-C, a hemorrhagic toxin from

the venom of Agkistrodon acutus, providing further evidence for the mechanism

of the pH-dependent proteolytic reaction of zinc metalloproteinases. Acta Cryst,

55: 1834-1841, 1999

• Ziolkowski C and Bieber AL: Mojave toxin affects fusion of myoblasts and

viability of myoblasts and viability of myotubes in cell cultures. Toxicon, 30: 733-

744, 1992

• Zucker MB: Platelet aggregation measured by photometric method. Meth

Enzymol, 169: 117-133, 1989