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

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.

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