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
Protein & Peptide Letters
Title: Cleavage Specificities of Aspartic Proteinases toward Oxidized Insulin B Chain At Different pH Values
Volume: 9 Issue: 4
Author(s): Senarath B. P. Athauda and Kenji Takahashi
Affiliation:
Keywords: Aspartic Proteinases, Oxidized Insulin, ionizable residues
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.
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Cite this article as:
Athauda B. P. Senarath and Takahashi Kenji, Cleavage Specificities of Aspartic Proteinases toward Oxidized Insulin B Chain At Different pH Values, Protein & Peptide Letters 2002; 9 (4) . https://dx.doi.org/10.2174/0929866023408698
DOI https://dx.doi.org/10.2174/0929866023408698 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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