Abstract
The proteolytic specificity of rhodostoxin, the major hemorrhagin from Calloselasma rhodostoma (Malayan pit viper) venom was investigated using oxidized B-chain of bovine insulin as substrate. Six peptide bonds were cleaved: Ser9-Hist10, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Gly20-Glu21 and Phe24-Phe25. Deglycosylated rhodostoxin, however, cleaved primarily at Arg22-Gly23.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Crotalid Venoms / metabolism*
-
Glycoproteins / metabolism*
-
Hemorrhage / chemically induced*
-
Hydrolysis
-
Metalloendopeptidases / metabolism*
-
Mice
-
Molecular Sequence Data
-
Substrate Specificity
Substances
-
Crotalid Venoms
-
Glycoproteins
-
rhodostoxin protein, Calloselasma rhodostoma
-
Metalloendopeptidases