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Article

Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity.

Biochemistry - 25 Aug 1992

Miyata T, Aruga R, Umeyama H, Bezeaud A, Guillin M C, Iwanaga S

Abstract excerpt

Structural studies on a hereditary abnormal prothrombin, prothrombin Salakta, have been performed to identify the difference responsible for its reduced fibrinogen clotting activity and its reduced esterase activity. Amino acid composition and sequence analyses of a peptide isolated from a lysylendopeptidase digest of the abnormal thrombin indicated that Glu-466 had been replaced by Ala. This amino acid...

Topics

Alanine
Amino Acid Sequence
Base Sequence
Codon
Esterases
Fibrinogen
Glutamates
Glutamic Acid
Humans
Models, Molecular
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Peptide Fragments

Protein Conformation

Prothrombin

Source

Identifiers

PMID: 1354985
DOI: 10.1021/bi00148a005

Genes

GCG

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1354985-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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