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

Purification and characterization of factor VIII 372-Cys: a hypofunctional cofactor from a patient with moderately severe hemophilia A.

Blood - 15 Apr 1990

O'Brien D P, Pattinson J K, Tuddenham E G

Abstract excerpt

We have purified factor VIII from a patient with moderately severe hemophilia A (FVIII, 4 U/dL; FVIII:Ag, 110 U/dL) and subjected the protein to Western blot analysis after time course activation with thrombin. The cross reacting material-positive (CRM+) FVIII has the normal distribution of heavy and light chains before thrombin activation, and, after incubation with the enzyme, appropriate cleavages are made at...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Blotting, Western
Share to Codon

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

Share to Cysteine

Share to Molecular Sequence Data

Share to Mutation

Share to Nucleic Acid Hybridization

Source

Identifiers

PMID: 2109644

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

Purification and characterization of factor VIII 372-Cys: a hypofunctional cofactor from a patient with moderately severe hemophilia A.PMID 2109644Read ↗

Partial reconstitution of factor VIII activity from a mild Crm+ hemophilia A patient by replacement of the defective A2 domain.Semantic proximity Read ↗

Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: evidence for nonproteolytic inactivation of factor VIIIa in vivo.Semantic proximity Read ↗

A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrates.Semantic proximity Read ↗

Functional mapping of the A2 domain from human factor VIII.Semantic proximity Read ↗

Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male.Semantic proximity Read ↗

Characterization of a factor IX variant with a glycine207 to glutamic acid mutation.Semantic proximity Read ↗

The molecular basis for cross-reacting material-positive hemophilia A due to missense mutations within the A2-domain of factor VIII.Semantic proximity Read ↗

Molecular and functional characterization of a natural homozygous Arg67His mutation in the prothrombin gene of a patient with a severe procoagulant defect contrasting with a mild hemorrhagic phenotype.Semantic proximity Read ↗

Molecular characterization of four novel mutations causing factor VII deficiency.Semantic proximity Read ↗

Factor VNew Brunswick: Ala221-to-Val substitution results in reduced cofactor activitySemantic proximity Read ↗

Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor.Semantic proximity Read ↗

A critical role for Gly25 in the B chain of human thrombin.Semantic proximity Read ↗

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