Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom.
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.
Tan
N H
NH
Department of Biochemistry, University of Malaya, Kuala Lumpur, Malaysia.
Ponnudurai
G
G
Chung
M C
MC
D000595:Amino Acid Sequence; D000818:Animals; D003435:Crotalid Venoms / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006470:Hemorrhage / Q000139:chemically induced*; D006868:Hydrolysis; D008666:Metalloendopeptidases / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D003435:Crotalid Venoms; D006023:Glycoproteins; C097743:rhodostoxin protein, Calloselasma rhodostoma; D008666:Metalloendopeptidases