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- W2068793497 abstract "A derivative of human blood clotting factor IXa beta lacking gamma-carboxyglutamic acid (Gla) residues was prepared by limited proteolysis with chymotrypsin, and subsequently examined for its ability to bind calcium ions. By amino acid analysis, Gla-domainless human factor IXa beta contained 0.3-0.4 moles of beta-hydroxyaspartic acid per mole of protein. Equilibrium dialysis experiments demonstrated that Gla-domainless human factor IXa beta retained two high-affinity calcium binding sites (Kd=52 microM), a finding essentially identical to that observed for Gla-domainless bovine factor IX that contains 0.8-0.9 moles of beta-hydroxyaspartic acid per mole of protein. These data strongly suggest that the beta-hydroxyaspartic acid residue in these proteins does not participate in their high affinity calcium sites." @default.
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- W2068793497 date "1985-07-01" @default.
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- W2068793497 title "Calcium binding to a human factor IXa derivative lacking γ-carboxyglutamic acid: Evidence for two high-affinity sites that do not involve β-hydroxyaspartic acid" @default.
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- W2068793497 doi "https://doi.org/10.1016/0006-291x(85)90493-0" @default.
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