Reichl A P, Serrano S M, Sampaio C A, Mandelbaum F R
Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, Brazil.
Toxicon. 1993 Nov;31(11):1479-82. doi: 10.1016/0041-0101(93)90213-3.
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).
测定了从莫氏矛头蝮蛇毒中分离出的三种碱性蛋白酶对氧化胰岛素B链的水解活性。丝氨酸蛋白酶MSP1和MSP2在相同位置以相同的键裂解顺序切割胰岛素B链。首先在Arg-Gly(22-23)位置发生裂解，随后是Lys-Ala(29-30)肽键的水解。金属蛋白酶MPB与丝氨酸蛋白酶不同，它能在四个位置非常迅速地切割胰岛素B链：Ser-His(9-10)、Ala-Leu(14-15)、Tyr-Leu(16-17)和Phe-Phe(24-25)。
