Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.
- 1 November 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (22) , 6934-6937
- https://doi.org/10.1073/pnas.81.22.6934
Abstract
Computer searches of the National Biomedical Research Foundation protein and nucleic acid sequence data bases using the NH2 terminus of the bovine factor Va 94-kilodalton H chain, the NH2 terminus of the 74-kilodalton factor Va L chain, and an internal 98-residue segment of porcine factor VIII revealed that both bovine factor V and porcine factor VIII are statistically homologous to human ceruloplasmin. The NH2-terminal segment of bovine factor Va H chain is homologous to 3 segments of ceruloplasmin sequence starting at residues 1, 351 and 713; the NH2-terminal sequence of bovine factor Va L chain is homologous to the same human ceruloplasmin sequence segments beginning at residues 1, 349 and 711. The longer porcine factor VIII sequence is homologous to 3 segments of human ceruloplasmin, residues 1-77, 400-433 and 683-791. The data indicate that factor V, factor VIII and ceruloplasmin comprise a group of evolutionarily linked protein structures that possibly resulted from multiplication of ancestral precursor genes.This publication has 16 references indexed in Scilit:
- Characterization of Factor V activation intermediates.Journal of Biological Chemistry, 1984
- Internal triplication in the structure of human ceruloplasmin.Proceedings of the National Academy of Sciences, 1983
- Thrombin-catalyzed activation of human coagulation factor V.Journal of Biological Chemistry, 1982
- Pattern recognition in nucleic acid sequences. I. A general method for finding local homologies and symmetriesNucleic Acids Research, 1982
- Similar Amino Acid Sequences: Chance or Common Ancestry?Science, 1981
- Coordinate binding of factor Va and factor Xa to the unstimulated platelet.Journal of Biological Chemistry, 1981
- [21] Factor VPublished by Elsevier ,1981
- The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity.Journal of Biological Chemistry, 1979
- Evidence for proteolytic fragments in commercial samples of human ceruloplasminFEBS Letters, 1971
- A general method applicable to the search for similarities in the amino acid sequence of two proteinsJournal of Molecular Biology, 1970