The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.

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Article

The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.

The Journal of biological chemistry - 25 Oct 1991

Van Deerlin V M, Tollefsen D M

Abstract excerpt

Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin and chymotrypsin. Inhibition occurs when the protease attacks the reactive site peptide bond in HCII (Leu444-Ser445) and becomes trapped as a covalent 1:1 complex. Dermatan sulfate and heparin increase the rate of inhibition of thrombin, but not of chymotrypsin, greater than 1000-fold. The N-terminal portion of HCII contains two...

Topics

Amino Acid Sequence
Animals
Binding Sites
Blotting, Western
Cattle
Chromatography, Liquid
Chymotrypsin
Electrophoresis, Polyacrylamide Gel
Female
Glycosaminoglycans
Heparin Cofactor II

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Humans

Hydrogen-Ion Concentration

Kinetics

Molecular Sequence Data

Mutation

Protease Inhibitors

Sequence Alignment

Source

Open in PubMed

Identifiers

PMID: 1939083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1939083-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.PMID 1939083Read ↗

Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition.Semantic proximity Read ↗

Arginine 200 of heparin cofactor II promotes intramolecular interactions of the acidic domain. Implication for thrombin inhibition.Semantic proximity Read ↗

Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.Semantic proximity Read ↗

Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.Semantic proximity Read ↗

Amino acid residues of heparin cofactor II required for stimulation of thrombin inhibition by sulphated polyanions.Semantic proximity Read ↗

Molecular mapping of the thrombin-heparin cofactor II complex.Semantic proximity Read ↗

Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.Semantic proximity Read ↗

Inhibition of a thrombin anion-binding exosite-2 mutant by the glycosaminoglycan-dependent serpins protein C inhibitor and heparin cofactor II.Semantic proximity Read ↗

Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance.Semantic proximity Read ↗

Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans.Semantic proximity Read ↗

Fucosylated chondroitin sulfate inhibits plasma thrombin generation via targeting of the factor IXa heparin-binding exosite.Semantic proximity Read ↗

Characterization of a heparin binding site on the heavy chain of factor XI.Semantic proximity Read ↗

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