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Article

Blood clotting factor IX Nagoya 3: the molecular defect of zymogen activation caused by an arginine-145 to histidine substitution.

Thrombosis research - 15 Nov 1990

Suehiro K, Miyata T, Takeya H, Takamatsu J, Saito H, Murakawa M, Okamura T, Niho Y, Iwanaga S

Abstract excerpt

Factor IX Nagoya 3 (IX Nagoya 3) is a natural mutant of factor IX recognized in a patient with moderately severe hemophilia B. The patient had 0.60 units/ml of factor IX antigen and 2-5% of clotting activity. IX Nagoya 3 was purified from the patient's plasma by immunoaffinity chromatography with an anti-factor IX monoclonal antibody column. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)...

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Source

Identifiers

PMID: 2087690
DOI: 10.1016/0049-3848(90)90109-p

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SDS

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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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Research trail→

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Blood clotting factor IX Nagoya 3: the molecular defect of zymogen activation caused by an arginine-145 to histidine substitution.PMID 2087690Read ↗

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

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Contributions of basic amino acids in the autolysis loop of factor XIa to serpin specificity.Semantic proximity Read ↗

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Characterization of the functional defect in factor IX Alabama. Evidence for a conformational change due to high affinity calcium binding in the first epidermal growth factor domain.Semantic proximity Read ↗

An important role for the activation peptide domain in controlling factor IX levels in the blood of haemophilia B mice.Semantic proximity Read ↗

Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa.Semantic proximity Read ↗

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