Factor VII C329R: A variant with a disrupted disulfide bond in the catalytic domain

H. L. James, K. D. Anderson, W. L. Nichols, J. A. Heit

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

We report a novel mutation within the coagulation factor VII gene associated with a dysfunctional procoagulant factor VII (12% of normal plasma factor VII activity; 50% of normal plasma factor VII antigen level). Using heteroduplex analysis and subsequent sequencing, we identified a thymine- 10,902 to cytosine mutation within exon eight of the factor VII gene, encoding for a substitution of arginine for cysteine-329 (factor VII C329R) within the heavy chain of factor VII. This substitution disrupts a disulfide bond within the factor VII catalytic domain and might cause altered conformation of the active site triad.

Original languageEnglish (US)
Pages (from-to)308-310
Number of pages3
JournalBlood Coagulation and Fibrinolysis
Volume8
Issue number5
DOIs
StatePublished - Jan 1 1997

Keywords

  • Factor VII
  • Genetic variant
  • Missense mutation

ASJC Scopus subject areas

  • Hematology

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