title: Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom.
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.
authors.affiliation: Department of Biochemistry, University of Malaya, Kuala Lumpur, Malaysia.
authors.forename: N H
authors.initials: NH
authors.lastname: Tan
authors.forename: G
authors.initials: G
authors.lastname: Ponnudurai
authors.forename: M C
authors.initials: MC
authors.lastname: Chung
mesh_terms: 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
chemical_list: D003435:Crotalid Venoms; D006023:Glycoproteins; C097743:rhodostoxin protein, Calloselasma rhodostoma; D008666:Metalloendopeptidases