A Comparison of Bovine Prothrombin, Factor IX (Christmas Factor), and Factor X (Stuart Factor)
- 1 February 1974
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (2) , 427-430
- https://doi.org/10.1073/pnas.71.2.427
Abstract
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.Keywords
This publication has 16 references indexed in Scilit:
- Isolation and characterization of bovine factor IX (Christmas factor)Biochemistry, 1973
- The activation of prothrombin III. The partial amino acid sequences at the amino terminal of prothrombin and the intermediates of activationBiochemical and Biophysical Research Communications, 1973
- A Form of Bovine Factor X with a Single Polypeptide ChainNature New Biology, 1973
- Bovine factors X1and X 2 (Stuart factor). Isolation and characterizationBiochemistry, 1972
- Characterization of two glycoprotein variants of bovine factor X and demonstration that the factor X zymogen contains two polypeptide chainsBiochemistry, 1972
- Bovine factor X1a (activated Stuart factor). Evidence of homology with mammalian serine proteasesBiochemistry, 1972
- Application of sequenator analysis to the study of proteinsBiochemistry, 1972
- The chromatographic determination of cystine and cysteine residues in proteins as s-beta-(4-pyridylethyl)cysteine.1970
- The isolation of undegraded bovine prothrombin and its partial characterizationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- N-Terminal Amino-Acids formed during the Activation of ProthrombinNature, 1962