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|Title:||Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom|
|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.|
|Appears in Collections:||Staff Publications|
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