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  • Title: Immunochemical studies of conformational alterations in bone gamma-carboxyglutamic acid containing protein.
    Author: Delmas PD, Stenner DD, Romberg RW, Riggs BL, Mann KG.
    Journal: Biochemistry; 1984 Sep 25; 23(20):4720-5. PubMed ID: 6333895.
    Abstract:
    The Ca2+-dependent transition of the vitamin K dependent bone protein bone Gla-containing protein (BGP) was investigated by use of anti-BGP antibody that reacts with the Ca2+-dependent conformation of BGP. Antibody binding occurred in the presence of Ca2+ or Mg2+ with a Kd(app) of 1.75 mM for Ca2+. Upon removal of Ca2+ with ethylenediaminetetraacetic acid, antibody binding was eliminated. Upon thermal acid decarboxylation of BGP, Ca2+-independent binding of the antibody was restored. Thus, the epitope not expressed by fully carboxylated BGP in the absence of calcium ion was restored either by addition of Ca2+ or by decarboxylation of the protein. Circular dichroic studies of fully carboxylated and fully decarboxylated BGP indicated that addition of Ca2+ to the fully carboxylated protein or decarboxylation to produce the glutamic acid containing equivalent of BGP resulted in increased order structure (apparent alpha-helix) in the protein, and this alteration was coincident with antibody binding. These data suggest that carboxylation of this vitamin K dependent protein may lead to increased disorder in the protein as compared to the glutamic acid containing equivalent. Upon Ca2+ binding a structure more equivalent to the Glu-containing protein is obtained.
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