Synthesis of lysine-containing sulphonium salts and their properties as proteinase inhibitors
- 15 March 1988
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 250 (3) , 871-876
- https://doi.org/10.1042/bj2500871
Abstract
Some sulphonium salts derived from lysine were synthesized with the general structure R-Lys-CH2S+-(alkyl)2. They were examined as inhibitors of the cysteine proteinase clostripain, which has a preference for cleaving peptide bonds at the carboxy group of basic amino acids, and of a number of trypsin-related serine proteinases. Clostripain was irreversibly inactivated by all reagents examined, but in the case of the serine proteinases, depending on the reagent structure, irreversible and reversible inhibitions were observed. These were kinetically characterized.This publication has 10 references indexed in Scilit:
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