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. 1985 Sep 1;230(2):497–502. doi: 10.1042/bj2300497

Specificity of activated human protein C.

S R Stone, J Hofsteenge
PMCID: PMC1152642  PMID: 3863616

Abstract

Peptide p-nitroanilide substrates and peptidylchloromethane inhibitors were used to examine the specificity of activated human Protein C. Substrates with arginine in the P1 position had the highest activity. The best substrates and inhibitors, as judged by the second-order rate constant for their interaction with the enzyme, had an apolar residue in the P2 position. In contrast with thrombin [Kettner & Shaw (1981) Methods Enzymol. 80, 826-842], activated Protein C was able to accommodate large hydrophobic residues such as phenylalanine and leucine in the P2 position. In the P3 position, the enzyme preferred an apolar D-amino acid residue. The results of the present study have also indicated a suitable substrate and inhibitor to be used in the assay of functional protein C and of thrombomodulin.

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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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