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. 1988 Mar 15;250(3):871–876. doi: 10.1042/bj2500871

Synthesis of lysine-containing sulphonium salts and their properties as proteinase inhibitors.

P Rauber 1, B Walker 1, S Stone 1, E Shaw 1
PMCID: PMC1148936  PMID: 2968789

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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