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A Comparison of Bovine Prothrombin, Factor IX (Christmas Factor), and Factor X (Stuart Factor)
Author(s) -
Kazuo Fujikawa,
Michael H. Coan,
David L. Enfield,
Koiti Titani,
Lowell H. Ericsson,
Earl W. Davie
Publication year - 1974
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.71.2.427
Subject(s) - factor x , factor ix , clotting factor , amino acid , factor v , factor vii , biology , peptide sequence , factor ixa , biochemistry , genetics , coagulation , gene , thrombin , immunology , medicine , platelet , thrombosis
A comparison has been made of the electrophoretic behavior, chemical composition, amino-terminal sequence, and immunological properties of bovine prothrombin, factor IX (Christmas factor), and factor X (Stuart factor). Some immunological crossreactivity was found between the antibody to prothrombin and factor X although prothrombin and factor X differ substantially in amino-acid and carbohydrate composition. Considerable amino-acid sequence homology was found in the amino-terminal portion of prothrombin, factor IX, and the light chain of factor X. These data provide further evidence to support the hypothesis that at least three of the vitamin K-dependent clotting factors have evolved from a common ancestral gene.

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