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  • Title: Partial characterization of a subtilisin inhibitor from black bean seeds.
    Author: Seidl DS, Abreu H, Jaffé WG.
    Journal: Int J Pept Protein Res; 1982 Feb; 19(2):153-7. PubMed ID: 6749728.
    Abstract:
    The subtilisin inhibitor (SI), isolated from black beans (Phaseolus vagaris) has a molecular weight of 8918 and it contains four half cystine residues. The N-terminal residue is arginine and the C-terminal is lysine. The subtilisin inhibiting site is composed of an Ala-Leu or Ile bond. This site interacts in addition to subtilisin (S) with elastase from human leukocytes (HLE), both of which compete for the inhibitor. Also, HLE-cleaved SI (SIHLE) is inactive against HLE as well as against S. It was shown that the inhibition of S by SI resembles a temporary inhibition, involving a very slow release of enzyme activity. The trypsin reactive site is a Lys-Val bond, and its interaction with bovine trypsin is very weak. No complexes of SI or trypsin-cleaved SI (SIT) with trypsin could be detected on cellulose-acetate membrane electrophoresis, while SIT forms a clearly visible complex with S.
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