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 Citations (Scopus)

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
StatePublished - 1997

Fingerprint

Factor VII
Disulfides
Catalytic Domain
Heteroduplex Analysis
Mutation
Thymine
Cytosine
Genes
Cysteine
Arginine
Exons
Antigens

Keywords

  • Factor VII
  • Genetic variant
  • Missense mutation

ASJC Scopus subject areas

  • Hematology

Cite this

James, H. L., Anderson, K. D., Nichols, W. L., & Heit, J. A. (1997). Factor VII C329R: A variant with a disrupted disulfide bond in the catalytic domain. Blood Coagulation and Fibrinolysis, 8(5), 308-310.

Factor VII C329R : A variant with a disrupted disulfide bond in the catalytic domain. / James, H. L.; Anderson, K. D.; Nichols, W. L.; Heit, J. A.

In: Blood Coagulation and Fibrinolysis, Vol. 8, No. 5, 1997, p. 308-310.

Research output: Contribution to journalArticle

James, HL, Anderson, KD, Nichols, WL & Heit, JA 1997, 'Factor VII C329R: A variant with a disrupted disulfide bond in the catalytic domain', Blood Coagulation and Fibrinolysis, vol. 8, no. 5, pp. 308-310.
James, H. L. ; Anderson, K. D. ; Nichols, W. L. ; Heit, J. A. / Factor VII C329R : A variant with a disrupted disulfide bond in the catalytic domain. In: Blood Coagulation and Fibrinolysis. 1997 ; Vol. 8, No. 5. pp. 308-310.
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