The sites of cleavage in oxidized insulin-B chain by a hemorrhagic protease derived from the venom of the habu (Trimeresurus flavoviridis).
The substrate specificity of a hemorrhagic protease derived from habu (Trimeresurus flavoviridis) venom was determined using oxidized insulin-B chain as a substrate. The enzyme was shown to be a fairly specific protease; it cleaved the substrate essentially at two positions, His10-Leu11 and Ala14-Leu15. The sites cleaved with the protease were compared to those reported with hemorrhagic proteases from other snake venoms.
Yamakawa
Y
Y
Department of Applied Immunology, National Institute of Health, Tokyo, Japan.
Omori-Satoh
T
T
D000818:Animals; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000032:analysis*; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis*; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism*; D010084:Oxidation-Reduction; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*
D003435:Crotalid Venoms; D007328:Insulin; D010450:Endopeptidases; D010447:Peptide Hydrolases; C039589:Ac1-proteinase