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  • Title: A mass spectrometric study of metal binding to osteocalcin.
    Author: Nousiainen M, Derrick PJ, Kaartinen MT, Mäenpää PH, Rouvinen J, Vainiotalo P.
    Journal: Chem Biol; 2002 Feb; 9(2):195-202. PubMed ID: 11880034.
    Abstract:
    Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry was used to investigate Ca(2+), Mg(2+), and La(3+) binding to bovine bone osteocalcin (OCN). OCN was shown to bind 3 mol Ca(2+) per mol protein. There was also evidence for the presence of four additional metal binding sites. Ca(2+) increased the formation of the OCN dimer. Mg(2+) bound to OCN to the same extent as Ca(2+) but did not induce the dimerization of OCN. La(3+) bound to a lesser extent than either Ca(2+) or Mg(2+) to OCN and, like Mg(2+), did not influence dimerization. Each Gla residue of OCN participates in Ca(2+) binding, whereas Mg(2+) binding may occur preferentially at sites other than Gla residues. This implies that the different natures of Ca(2+)- and Mg(2+)-containing OCN complexes influence the tendency of OCN to form a dimer.
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