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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Cleavage Specificities of Aspartic Proteinases toward Oxidized Insulin B Chain At Different pH Values

Author(s): Senarath B. P. Athauda and Kenji Takahashi

Volume 9 , Issue 4 , 2002

Page: [289 - 294] Pages: 6

DOI: 10.2174/0929866023408698

Price: $65

Abstract

The cleavage specificities of typical aspartic proteinases: pepsin A, gastricsin, cathepsin D and rhizopuspepsin,were examined at different pH values with oxidized insulin B chain as a substrate with special attention to the specificities near neutral pH. Significant differences in relative specificity for scissile bonds were observed between pH 2.0 and 5.5-6.5, which may be partly related with the changes in dissociation states of the His and Glu residues in the substrate and the ionizable residues in the active site of each enzyme.

Keywords: Aspartic Proteinases, Oxidized Insulin, ionizable residues


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