volume 16, issue 7, P596-601 1994
DOI: 10.1016/0141-0229(94)90125-2
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Václav Čeěovský, Hans-Dieter Jakubke

Abstract: The characterization of the S' subsite specificity of native and ethylated alpha-chymotrypsin has been studied via acyl transfer reaction in acetonitrile containing 10 vol% of water. Using Ac-Tyr-OEt as acyl donor, we investigated the partitioning of acyl-chymotrypsins between water and amino acid and peptide-derived nucleophiles. For the investigation of S'2 subsite specificity, a series of 19 dipeptides of the general structure Ala-Xaa (Xaa represents all natural amino acids except cysteine) were used. From …

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