The interaction of prothrombin with phospholipid membranes is independent of either kringle domain.

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Article

The interaction of prothrombin with phospholipid membranes is independent of either kringle domain.

The Journal of biological chemistry - 25 Jul 1993

Kotkow K J, Furie B, Furie B C

Abstract excerpt

Prothrombin contains two kringle domains, a structural motif common to other plasma proteins involved in hemostasis and fibrinolysis. To determine the role of the kringle domains of prothrombin, we prepared three recombinant human prothrombin forms lacking the first kringle domain (residues 63-14...

Topics

1-Carboxyglutamic Acid
Animals
Base Sequence
Binding Sites
CHO Cells
Calcium
Chromatography, Gel
Cloning, Molecular
Cricetinae
Electrophoresis, Polyacrylamide Gel
Humans
Membrane Lipids
Molecular Sequence Data
Mutation
Oligodeoxyribonucleotides
Peptide Fragments
Phospholipids
Protein Conformation

Source

Open in PubMed

Identifiers

PMID: 8393451

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8393451-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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