Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Distinct binding sites of Ala48-hirudin1-47 and Ala48-hirudin48-65 on alpha-thrombin.

The Journal of biological chemistry - 15 Jan 1990

Dodt J, Köhler S, Schmitz T, Wilhelm B

Abstract excerpt

The interaction of alpha-thrombin with Ala48-hirudin, Ala48-hirudin1-47, and Ala48-hirudin48-65 was analyzed. Mutations at Pro48 were found to cause only slight changes in the kon (human: 3.1 +/- 0.3 x 10(8) M-1 s-1; bovine: 1.03 +/- 0.3 x 10(8) M-1 s-1) and koff (human: 0.4 +/- 0.2 x 10(-3) s-1; bovine: 2.9 +/- 0.4 x 10(-3) s-1) rate constants for the formation of the thrombin-hirudin complex. The amino-terminal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alanine
Share to Amino Acid Sequence
Share to Cattle

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Chromatography, High Pressure Liquid

Share to Electrophoresis, Polyacrylamide Gel

Share to Molecular Sequence Data

Share to Mutation

Share to Proline

Source

Identifiers

PMID: 2295615

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Distinct binding sites of Ala48-hirudin1-47 and Ala48-hirudin48-65 on alpha-thrombin.PMID 2295615Read ↗

Hirudin binding reveals key determinants of thrombin allostery.Semantic proximity Read ↗

Probing the distance between the two binding sites of hirudin for its interaction with the active site and the fibrin(ogen)-binding site of alpha-thrombin.Semantic proximity Read ↗

Hirudin: amino-terminal residues play a major role in the interaction with thrombin.Semantic proximity Read ↗

Binding of hirudin to meizothrombin.Semantic proximity Read ↗

Use of fragments of hirudin to investigate thrombin-hirudin interaction.Semantic proximity Read ↗

Fusion of the C-terminal triskaidecapeptide of hirudin variant 3 to alpha1-proteinase inhibitor M358R increases the serpin-mediated rate of thrombin inhibition.Semantic proximity Read ↗

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

Mutagenesis studies toward understanding allostery in thrombin.Semantic proximity Read ↗

Thrombin hydrolysis of human osteopontin is dependent on thrombin anion-binding exosites.Semantic proximity Read ↗

Acidic Region Residues 1680-1684 in the A3 Domain of Factor VIII Contain a Thrombin-Interactive Site Responsible for Proteolytic Cleavage at Arg1689.Semantic proximity Read ↗

Recombinant hirudin: kinetic mechanism for the inhibition of human thrombin.Semantic proximity Read ↗

The 95RGD97 sequence on the Aα chain of fibrinogen is essential for binding to its erythrocyte receptor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.