Hydrolytic specificity of three basic proteinases isolated from the venom of Bothrops moojeni for the B-chain of oxidized insulin.
The hydrolytic activity of three basic proteinases isolated from Bothrops moojeni venom was determined on the B-chain of oxidized insulin. The serine proteinases MSP1 and MSP2 cleave the insulin B-chain at identical positions and in the same order of bond cleavage. Cleavage occurs first at the Arg-Gly(22-23) position, followed by hydrolysis of the Lys-Ala(29-30) peptide bond. The metalloproteinase MPB differs from the serine proteinases in cleaving the insulin B-chain very rapidly at four positions: Ser-His(9-10), Ala-Leu(14-15), Tyr-Leu(16-17) and Phe-Phe(24-25).
Reichl
A P
AP
Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, Brazil.
Serrano
S M
SM
Sampaio
C A
CA
Mandelbaum
F R
FR
D000595:Amino Acid Sequence; D000818:Animals; D017837:Bothrops; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000201:enzymology*; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000378:metabolism*; D045726:Metalloproteases; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000378:metabolism*
D003435:Crotalid Venoms; D007328:Insulin; D045726:Metalloproteases; C578709:moojenin, Bothrops moojeni; C081402:MSP 1 proteinase, Bothrops moojeni; C081403:MSP 2 proteinase, Bothrops moojeni; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases