| Literature DB >> 9241791 |
N H Tan1, G Ponnudurai, M C Chung.
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.Entities:
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Year: 1997 PMID： 9241791 DOI： 10.1016/s0041-0101(96)00186-9
Source DB: PubMed Journal: Toxicon ISSN： 0041-0101 Impact factor: 3.033