The effect of divalent metal ions on the electrophoretic mobility of bovine prothrombin and bovine prothrombin fragment 1

D. W. Deerfield, P. Berkowitz, D. L. Olson, S. Wells, R. A. Hoke, K. A. Koehler, L. G. Pedersen, R. G. Hiskey

Research output: Contribution to journalArticle

Abstract

Examination of metal ion-dependent effects on the electrophoretic mobility of bovine prothrombin and fragment 1 provides a useful and sensitive method for investigation of conformational processes in these proteins. Utilization of this method reveals a conformational change in bovine prothrombin and fragment 1 which occurs at low metal ion concentrations. Equilibrium dialysis studies indicate that the metal ion-induced shape change occurs concomitant with binding of a single calcium ion/molecule of prothrombin or fragment 1. Mixed metal electrophoretic mobility studies with Mg2+ and Ca2+ have demonstrated the 'synergistic' effect for fragment 1 observed by others. Mixed metal equilibrium dialysis has provided experimental support for this observation and allows us to conclude that two tight Ca2+ sites are not affected by low Mg2+ concentrations and that the third Ca2+ site is also a tight site for Mg2+. Thus, at low Mg2+ concentrations and upon the addition of Ca2+, there are effectively three tight sites; consequently more Ca2+ will bind to the protein at lower total Ca2+ ion concentrations.

Original languageEnglish (US)
Pages (from-to)4833-4839
Number of pages7
JournalJournal of Biological Chemistry
Volume261
Issue number11
StatePublished - 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Deerfield, D. W., Berkowitz, P., Olson, D. L., Wells, S., Hoke, R. A., Koehler, K. A., Pedersen, L. G., & Hiskey, R. G. (1986). The effect of divalent metal ions on the electrophoretic mobility of bovine prothrombin and bovine prothrombin fragment 1. Journal of Biological Chemistry, 261(11), 4833-4839.