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Article

Impact of mutations at the P4 and P5 positions on the reaction of antithrombin with thrombin and elastase.

Thrombosis research - 15 Oct 1997

Cunningham M A, Blajchman M A, Sheffield W P

Abstract excerpt

Antithrombin (AT) is a serpin capable of trapping thrombin (IIa) in a stable and covalent complex. Complex formation is prevented by leukocyte elastase (LE) cleavage near the AT reactive centre. We mutated the known LE cleavage sites of AT to explore the possibility of producing an LE-resistant AT molecule. Initially, six rabbit AT variants differing only at residue 390 (P4) were generated in a cell-free system,...

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Identifiers

PMID: 9361370
DOI: 10.1016/s0049-3848(97)00228-4

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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