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Article

Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.

The Journal of biological chemistry - 24 Sept 1999

Liaw P C, Austin R C, Fredenburgh J C, Stafford A R, Weitz J I

Abstract excerpt

Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin. To explore this model of activation, we systematically substituted basic residues in the glycosaminoglycan-binding domain of HCII with neutral amino acids and measured the rates of thrombin inactivation by the mutants. Mutant D, with changes at...

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Identifiers

PMID: 10488098
DOI: 10.1074/jbc.274.39.27597

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.PMID 10488098Read ↗

The preferred pathway of glycosaminoglycan-accelerated inactivation of thrombin by heparin cofactor II.Semantic proximity Read ↗

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

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

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

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 ↗

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

Selective disruption of heparin and antithrombin-mediated regulation of human factor IX.Semantic proximity Read ↗

Reformable intramolecular cross-linking of the N-terminal domain of heparin cofactor II: effects on enzyme inhibition.Semantic proximity Read ↗

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