Abstract
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).
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