Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0041-0101(96)00186-9
Title: Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom
Authors: Tan, N.-H.
Ponnudurai, G.
Chung, M.C.M. 
Issue Date: Jun-1997
Source: Tan, N.-H., Ponnudurai, G., Chung, M.C.M. (1997-06). Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom. Toxicon 35 (6) : 979-984. ScholarBank@NUS Repository. https://doi.org/10.1016/S0041-0101(96)00186-9
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: 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 rhodostoxin, however, cleaved primarily at Arg 22-Gly 23.
Source Title: Toxicon
URI: http://scholarbank.nus.edu.sg/handle/10635/107768
ISSN: 00410101
DOI: 10.1016/S0041-0101(96)00186-9
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