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Thromb Haemost 1978; 40(02): 350-357
DOI: 10.1055/s-0038-1648668
Original Article
Schattauer GmbH Stuttgart

The Binding of Calcium Ions to Bovine Factor X by Rate Dialysis

Robert H Yue
The Cardiovascular Research Division, Institute of Rehabilitation Medicine, New York University Medical Center, New York, New York/10016, USA
,
Menard M Gertler
The Cardiovascular Research Division, Institute of Rehabilitation Medicine, New York University Medical Center, New York, New York/10016, USA
› Author Affiliations
Further Information

Publication History

Received 28 September 1977

Accepted 28 December 1977

Publication Date:
12 July 2018 (online)

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Summary

The binding of Ca+2 to bovine factor X (molecular weight of 74,000) (Yue und Gertler 1977) was studied by the technique of rate dialysis and with the use of 45Ca+2. The binding data are consistent with a model of sequential mechanism. One mole of Ca+2 binds to the glycoprotein with a dissociation constant of 5.2 × 10-5 M and an additional 39 ± 4 moles of Ca+2 bind to this zymogen with a dissociation constant of 3.7 × 10-3M. The binding of the high affinity Ca+2 causes a functionally significant change in the zymogen, and (calcium) (factor X) complex is the real substrate in the activation process by the protease in Russell’s viper venom.

 

  • References

  • 1 Colowick SP, Womack EC. 1969; Binding of diffusible molecules by macromolecules: rapid measurement by rate dialysis. Journal of Biological Chemistry 244: 774
    PubMedGoogle Scholar
  • 2 Davie EW, Ratnoff OD. 1964; Waterfall sequence for intrinsic blood clotting. Science 145: 1310
    CrossrefPubMedGoogle Scholar
  • 3 Davie EW, Kirby EP. 1973; Molecular mechanisms in blood coagulation. Current topics in cellular regulation 7: 51
    PubMedGoogle Scholar
  • 4 Davie EW, Fujikawa K. 1975; Basic mechanisms in blood coagulation. Annual Review of Biochemistry 44: 799
    CrossrefPubMedGoogle Scholar
  • 5 Dombrose FA, Seegers WH. 1973; Evidence for multiple molecular forms of autoprothrombin C (factor Xa). Thrombosis Research 3: 737
    CrossrefPubMedGoogle Scholar
  • 6 Esnouf MP, Macfarlane RG. 1968; Enzymology and the blood clotting mechanism. Advances in Enzymology 30: 255
    PubMedGoogle Scholar
  • 7 Esnouf MP, Williams WJ. 1962; The isolation and purification of a bovine-plasma protein which is a substrate for the coagulant fraction of Russell’s viper venom. Biochemical Journal 84: 62
    CrossrefPubMedGoogle Scholar
  • 8 Fujikawa K, Coan MH, Legaz ME, Davie EW. 1974; The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways. Biochemistry 13: 5290
    CrossrefPubMedGoogle Scholar
  • 9 Fujikawa K, Legaz ME, Davie EW. 1972; Bovine factor (Stuart factor). Mechanism of activation by a protein from Russell’s viper venom Biochemistry 11: 4892
    CrossrefPubMedGoogle Scholar
  • 10 Furie B, Furie BC. 1976; Spectral changes in bovine factor X associated with activation by the venom coagulant protein of Vipera Russelli. Journal of Biological Chemistry 251: 6807
    PubMedGoogle Scholar
  • 11 Henriksen RA, Jackson CM. 1975; The chemistry and enzymology of bovine factor X. Seminars in Thrombosis and Hemostasis 1: 284
    Article in Thieme ConnectPubMedGoogle Scholar
  • 12 Hummel BC W. 1959; A modified spectrophotometric determination of Chymotrypsin, trypsin and thrombin. Canadian Journal of Biochemistry and Physiology 37: 1393
    CrossrefPubMedGoogle Scholar
  • 13 Jackson CM, Hanahan DJ. 1968; Studies of bovine factor X. II. Characterization of purified factor X. Observation on some alteration in zone electrophoretic and chromatographic behavior occurring during purification Biochemistry 7: 4506
    CrossrefPubMedGoogle Scholar
  • 14 Jesty J, Spencer AK, Nemerson Y. 1974; The mechanism of activation of factor X. Kinetic control of alternative pathways leading to the formation of activated factor X. Journal of Biological Chemistry 249: 5614
    PubMedGoogle Scholar
  • 15 Jesty J, Spencer AK, Nakashima Y, Nemerson Y, Konigsberg W. 1975; The activation of coagulation factor X. Journal of Biological Chemistry 250: 4497
    PubMedGoogle Scholar
  • 16 Kuby SA, Noltmann EA. 1962. ATP-creatine transphosphorylase. In: Boyer PD, Lardy HA, Myrback K. (eds.) The Enzymes. 6 Academic Press; New York: p 515
    Google Scholar
  • 17 Lechner K, Deutsch E. 1965; Activation of factor X. Thrombosis et Diathesis Haemorrhagica 13: 314
    PubMedGoogle Scholar
  • 18 Macfarlane RG. 1964; An enzyme cascade in the blood clotting mechanism and its function as a biochemical amplifier. Nature 202: 498
    CrossrefPubMedGoogle Scholar
  • 19 Marciniak E, Seegers WH. 1965; Experiments with prothrombin, prethrombin, autoprothrombin III and plasmas with prothrombin related deficiencies. New Istanbul Contribution to Clinical Science 8: 117
    PubMedGoogle Scholar
  • 20 Netsestuen GL, Broderius M, Martin G. 1976; Role of γ-carboxyglutamic acid. Cation specificity of prothrombin factor X-phospholipid binding Journal of Biological Chemistry 251: 6886
    PubMedGoogle Scholar
  • 21 Osborne J, Lunasin A, Steiner RF. 1972; The binding of calcium by chymotrypsinogen A. Biochimica et biophysica acta 49: 923
    PubMedGoogle Scholar
  • 22 Radcliffe RD, Barton PG. 1972; The purification and properties of activated factor X. Bovine factor X activated with Russell’s viper venom Journal of Biological Chemistry 247: 7735
    PubMedGoogle Scholar
  • 23 Ridlington JW, Butler L. 1969; Measurement of binding of phosphate ligands to ribonucléase A by direct and competitive dialysis rate technique. Journal of Biological Chemistry 244: 111
    PubMedGoogle Scholar
  • 24 Ridlington JW, Butler L. 1972; Yeast inorganic pyrophosphatase. I. Binding of pyrophosphate, metal ion, and metal ionpyrophosphate complexes. Journal of Biological Chemistry 247: 7303
    PubMedGoogle Scholar
  • 25 Sakuragawa N, Mccoy LE, Seegers WH. 1972; Some effects of calcium and strontium ions on three basic reactions of blood coagulation. Thrombosis et Diathesis Haemorrhagica 27: 234
    PubMedGoogle Scholar
  • 26 Scatchard G. 1949; The attractions of protein for small molecules and ions. Annals of the New York Academy of Science 51: 660
    CrossrefPubMedGoogle Scholar
  • 26 Seegers WH. 1962. Prothrombin. Harvard University Press; Cambridge, Massachusetts:
    Google Scholar
  • 27 Seegers WH. 1967. Blood Clotting Enzymology. Academic Press; New York and London:
    Google Scholar
  • 28 Watts DC. 1973. Creatine kinase (adenosine 5’-triphosphate-creatine phosphotransferase). In: Boyer PD. (ed.) The Enzymes, Vol. VIII, Pt. A. 3rd. Ed. Academic Press; New York: p 383
    Google Scholar
  • 29 Yue RH, Gertler MM. 1977; Isolation of the high molecular form of bovine factor X and some of its physical properties. Biochimica et biophysica acta 490: 350
    CrossrefPubMedGoogle Scholar
  • 30 Yue RH, Noltmann EA, Kuby SA. 1969; Glucose 6-Phosphate Dehydrogenase from Brewers’ Yeast (Zwischenferment). Journal of Biological Chemistry 244: 1353
    PubMedGoogle Scholar