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Article

Analysis of fibrinogen A alpha-fusion proteins. Mutants which inhibit thrombin equivalently are not equally good substrates.

The Journal of biological chemistry - 15 Jan 1990

Lord S T, Byrd P A, Hede K L, Wei C, Colby T J

Abstract excerpt

We have examined the interaction of thrombin with fibrinogen A alpha chain residues 7-16. Using genetically engineered constructions, we have synthesized in Escherichia coli a fibrinogen A alpha 1-50 fusion protein and seven mutant proteins with single amino acid substitutions. These are: Asp7----Ala, Phe8----Tyr, Glu11----Ala, Gly12----Val, Gly13----Val, Gly14----Val, and Arg16----Leu. Competitive immunoassay of...

Topics

Amino Acid Sequence
Amino Acids
Base Sequence
Catalysis
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Escherichia coli
Fibrinogen
Fibrinopeptide A
Kinetics
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Plasmids

Recombinant Fusion Proteins

Substrate Specificity

Thrombin

Source

Identifiers

PMID: 2404012

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2404012-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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