PROTEOLYTIC SPECIFICITY OF RHODOSTOXIN, THE MAJOR HEMORRHAGIN OF CALLOSELASMA-RHODOSTOMA (MALAYAN PIT VIPER) VENOM

Authors
TAN NH PONNUDURAI G CHUNG MCM
Citation
Nh. Tan et al., PROTEOLYTIC SPECIFICITY OF RHODOSTOXIN, THE MAJOR HEMORRHAGIN OF CALLOSELASMA-RHODOSTOMA (MALAYAN PIT VIPER) VENOM, Toxicon, 35(6), 1997, pp. 979-984
Citations number
26
Categorie Soggetti
Toxicology,"Pharmacology & Pharmacy
Journal title
Toxicon → ACNP
ISSN journal
00410101
Volume
35
Issue
6
Year of publication
1997
Pages
979 - 984
Database
ISI
SICI code
0041-0101(1997)35:6<979:PSORTM>2.0.ZU;2-0
Abstract
The proteolytic specificity of rhodostoxin, the major hemorrhagin from Calloselasma rhodostoma (Malayan pit viper) venom was investigated us ing oxidized B-chain of bovine insulin as substrate. Six peptide bonds were cleaved: Ser(9)-Hist(10), His(10)-Leu(11), Ala(14)-Leu(15), Tyr( 16)-Leu(17), Gly(20)-Glu(21) and Phe(24)-Phe(25). Deglycosylated rhodo stoxin, however,cleaved primarily at Arg(22)-Gly(23). (C) 1997 Elsevie r Science Ltd.