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The specificity of peptide bond cleavage of acid proteinase A from Aspergillus niger var. macrosporus toward oxidized ribonuclease A.

作者信息

Takahashi K

机构信息

Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.

出版信息

Biosci Biotechnol Biochem. 1997 Feb;61(2):381-3. doi: 10.1271/bbb.61.381.

DOI:10.1271/bbb.61.381
PMID:9058983
Abstract

In order to investigate the specificity of peptide bond cleavage by acid proteinase A from Aspergillus niger var. macrosporus (Aspergillopepsin II), performic acid-oxidized bovine pancreatic ribonuclease A was digested by the enzyme at pH 1.8 or 5.5, and the resulting peptides were separated by HPLC and analyzed. Among the total 123 peptide bonds approximately thirty and thirteen bonds were cleaved at pH 1.8 for 2 h and at pH 5.5 for 20 h, respectively. Cleavages occurred fairly specifically at Tyr-X, Phe-X, His-X, Asn-X, Asp-X, Gln-X, and Glu-X bonds.

摘要

相似文献

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