Home LiteratureArticle Details
PMID: 1055402 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Isolation and characterization of vitamin K-dependent region of bovine blood clotting factor X.

Howard JB, Nelsestuen GL

Abstract

A 39-residue peptide from the tryptic digestion of bovine blood clotting factor X has been isolated by specific adsorption on barium citrate. The amino- and carboxyl-terminal sequences of the peptide were determined and compared to the vitamin K-dependent Ca2+-binding region from bovine prothrombin. The factor X peptide was found to contain gamma-carboxyglutamic acid residues, and the results of independent analysis are consistent with all 14 glutamic acid residues as gamma-carboxyglutamic acid. The similarity of the factor X peptide to the prothrombin peptide supports the hypothesis that the vitamin K-dependent blood clotting proteins are descended from a common ancestral gene.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Binding Sites Calcium Cattle Chromatography, Ion Exchange Factor X/isolation & purification Peptide Fragments Protein Binding Receptors, Drug Trypsin Vitamin K
Chemicals
Amino Acids Peptide Fragments Receptors, Drug Vitamin K Factor X Trypsin Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Howard J B
Nelsestuen G L
References (24)
24 references, click to expand
  1. A study of the reaction product of factor 8 and factor IX by gel filtration.
    Thromb Diath Haemorrh. 1967 Aug 15;18(1-2):211-22 PMID: 6071104
  2. THE ACTIVATION OF ANTIHEMOPHILIC FACTOR (FACTOR 8) BY ACTIVATED CHRISTMAS FACTOR (ACTIVATED FACTOR9 9).
    Biochemistry. 1964 Nov;3:1720-5 PMID: 14240634
  3. OBSERVATIONS ON THE INTERACTION OF PHOSPHOLIPIDS AND CERTAIN CLOTTING FACTORS IN PROTHROMBIN ACTIVATOR FORMATION.
    Biochim Biophys Acta. 1964 Aug 19;90:436-9 PMID: 14220741
  4. The Stuart-Prower factor assay and its clinical significance.
    Thromb Diath Haemorrh. 1958 May 1;2(1-2):24-38 PMID: 13581015
  5. Vitamin K dependent modifications of glutamic acid residues in prothrombin.
    Proc Natl Acad Sci U S A. 1974 Jul;71(7):2730-3 PMID: 4528109
  6. Bovine factor X 1a (activated Stuart factor). Evidence of homology with mammalian serine proteases.
    Biochemistry. 1972 Dec 19;11(26):4899-903 PMID: 4264286
  7. Bovine factor X 1 (Stuart factor). Mechanism of activation by protein from Russell's viper venom.
    Biochemistry. 1972 Dec 19;11(26):4892-9 PMID: 4674072
  8. The carbohydrate of bovine prothrombin. Partial structural determination demonstrating the presence of -galactose residues.
    J Biol Chem. 1972 Oct 10;247(19):6096-102 PMID: 4631316
  9. Mode of action of vitamin K. Calcium binding properties of bovine prothrombin.
    Biochemistry. 1972 Dec 19;11(26):4961-4 PMID: 4118102
  10. Vitamin K and the biosynthesis of prothrombin. 3. Structural comparison of an NH2-terminal fragment from normal and from dicoumarol-induced bovine prothrombin.
    J Biol Chem. 1973 Sep 25;248(18):6325-32 PMID: 4125867
  11. The purification and properties of an abnormal prothrombin protein produced by dicumarol-treated cows. A comparison to normal prothrombin.
    J Biol Chem. 1972 Dec 25;247(24):8176-82 PMID: 4118354
  12. The mode of action of vitamin K. Identification of gamma-carboxyglutamic acid as a component of prothrombin.
    J Biol Chem. 1974 Oct 10;249(19):6347-50 PMID: 4214105
  13. A comparison of bovine prothrombin, factor IX (Christmas factor), and factor X (Stuart factor).
    Proc Natl Acad Sci U S A. 1974 Feb;71(2):427-30 PMID: 4205592
  14. Determination of the amino acid sequence of the monkey, sheep, and dog proinsulin C-peptides by a semi-micro Edman degradation procedure.
    J Biol Chem. 1972 Aug 10;247(15):4866-71 PMID: 4626369
  15. Bovine factors X 1 and X 2 (Stuart factor). Isolation and characterization.
    Biochemistry. 1972 Dec 19;11(26):4882-91 PMID: 4629382
  16. A polypeptide region of bovine prothrombin specific for binding to phospholipids.
    Proc Natl Acad Sci U S A. 1973 May;70(5):1344-8 PMID: 4514304
  17. The mode of action of vitamin K. Isolation of a peptide containing the vitamin K-dependent portion of prothrombin.
    Proc Natl Acad Sci U S A. 1973 Dec;70(12):3366-70 PMID: 4519629
  18. The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent).
    Biochemistry. 1974 Oct 22;13(22):4508-16 PMID: 4473201
  19. Properties of a Ca2+ binding peptide from prothrombin.
    Biochem Biophys Res Commun. 1974 Jul 24;59(2):757-63 PMID: 4853901
  20. Isolation and characterization of bovine factor IX (Christmas factor).
    Biochemistry. 1973 Nov 20;12(24):4938-45 PMID: 4796921
  21. The activation of prothrombin. II. Partial reactions, physical and chemical characterization of the intermediates of activation.
    J Biol Chem. 1973 Oct 25;248(20):7149-63 PMID: 4743518
  22. Characterization of two glycoprotein variants of bovine factor X and demonstration that the factor X zymogen contains two polypeptide chains.
    Biochemistry. 1972 Dec 19;11(26):4873-82 PMID: 4638344
  23. Strategy and tactics in protein chemistry.
    Biochem J. 1970 Oct;119(5):805-22 PMID: 4923920
  24. Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac.
    Biochemistry. 1971 Dec 21;10(26):4912-21 PMID: 5134536
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1975-04-00
Pages
1281-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC432516
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]