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Article

Substitution of valine for leucine 305 in factor VIIa increases the intrinsic enzymatic activity.

The Journal of biological chemistry - 3 Aug 2001

Persson E, Bak H, Olsen O H

Abstract excerpt

Factor VII requires the cleavage of an internal peptide bond and the association with tissue factor (TF) to attain its fully active factor VIIa (FVIIa) conformation. The former event alone leaves FVIIa in a zymogen-like state of relatively low specific activity. We have designed a number of FVIIa...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11389142
DOI: 10.1074/jbc.M102187200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11389142-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Substitution of valine for leucine 305 in factor VIIa increases the intrinsic enzymatic activity.PMID 11389142Read ↗

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