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Article

Comparative trajectories of active and S195A inactive trypsin upon binding to serpins.

The Journal of biological chemistry - 11 Oct 2002

Mellet Philippe, Mély Yves, Hedstrom Lizbeth, Cahoon Marguerite, Belorgey Didier, Srividya Narayanan, Rubin Harvey, Bieth Joseph G

Abstract excerpt

Serpins inhibit proteinases through a complicated multistep mechanism. The precise nature of these steps and the order by which they occur are still debated. We compared the fate of active and S195A inactive rat trypsin upon binding to alpha(1)-antitrypsin and P(1)-Arg-antichymotrypsin using stopped-flow kinetics with fluorescence resonance energy transfer detection and time-resolved fluorescence resonance energy...

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Identifiers

PMID: 12077135
DOI: 10.1074/jbc.M204090200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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