HYDROLYTIC SPECIFICITY OF 3 BASIC PROTEINASES ISOLATED FROM THE VENOMOF BOTHROPS-MOOJENI FOR THE B-CHAIN OF OXIDIZED INSULIN

Authors
REICHL AP SERRANO SMT SAMPAIO CAM MANDELBAUM FR
Citation
Ap. Reichl et al., HYDROLYTIC SPECIFICITY OF 3 BASIC PROTEINASES ISOLATED FROM THE VENOMOF BOTHROPS-MOOJENI FOR THE B-CHAIN OF OXIDIZED INSULIN, Toxicon, 31(11), 1993, pp. 1479-1482
Citations number
8
Categorie Soggetti
Toxicology,"Pharmacology & Pharmacy
Journal title
Toxicon → ACNP
ISSN journal
00410101
Volume
31
Issue
11
Year of publication
1993
Pages
1479 - 1482
Database
ISI
SICI code
0041-0101(1993)31:11<1479:HSO3BP>2.0.ZU;2-X
Abstract
The hydrolytic activity of three basic proteinases isolated from Bothr ops moojeni venom was determined on the B-chain of oxidized insulin. T he serine proteinases MSP1 and MSP2 cleave the insulin B-chain at iden tical positions and in the same order of bond cleavage. Cleavage occur s first at the Arg-Gly(22-23) position, followed by hydrolysis of the Lys-Ala(29-30) peptide bond. The metalloproteinase MPB differs from th e serine proteinases in cleaving the insulin B-chain very rapidly at f our positions: Ser-His(9-10), Ala-Leu(14-15), Tyr-Leu(16-17) and Phe-P he(24-25).