| Literature DB >> 3942751 |
V Schellenberger, H D Jakubke.
Abstract
The partitioning of maleylphenylalanine-alpha-chymotrypsin formed using maleylphenylalanine methyl ester as acyl donor between amino acid-derived nucleophiles and water was determined spectrophotometrically. The interpretation of the results obtained from graphical analysis gave evidence of a high conformational specificity of alpha-chymotrypsin towards basic amino acid derivatives in the P'1 position including significant differences between the amide and methyl ester of arginine. Amides of neutral amino acids with large side-chains show higher nucleophile reactivity in comparison with glycine amide.Entities:
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Year: 1986 PMID： 3942751 DOI： 10.1016/0167-4838(86)90309-2
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002