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Human serum histidine rich glyco protein part 1 interactions with heme metal ions and organic ligands


, : Human serum histidine rich glyco protein part 1 interactions with heme metal ions and organic ligands. Biochimica et Biophysica Acta 535(2): 319-333

The 3.8 S .alpha.2-histidine-rich glycoprotein of human serum is composed of 2 non-identical subunits, each of which contains carbohydrate. The far UV circular dichroism spectrum of .alpha.2-histidine-rich glycoprotein indicates that the protein has little .alpha.-helix but apparently appreciable amounts of .beta.-sheet and non-regular structures. .alpha.2-Histidine-rich glycoprotein binds heme with concomitant changes in the electrophoretic mobility of the protein, in the fluorescence of tryptophan residues and in the absorption and optical activity of the heme chromophore. By fluorescence quenching, the stoichiometry of binding is 1 heme/.alpha.2-histidine-rich glycoprotein molecule with an apparent Kd near 1.5 .mu.M; however, by changes in absorbance, the interaction of 9-10 additional heme molecules with the .alpha. protein can be detected. The absorption spectra of heme.cntdot.alpha.2-histidine-rich glycoprotein complexes resemble those of low-spin hemoproteins. The ellipticity induced in the heme chromophore on binding by .alpha.2-histidine-rich glycoprotein increases linearly up to about 10 hemes bound per mol protein. No change in the conformation of .alpha.2-histidine-rich glycoprotein was indicated by circular dichroism when 1 or 2 heme molecules are bound by the protein. .alpha.2-Histidine-rich glycoprotein does not effectively compete with human serum albumin for heme, suggesting that .alpha.2-histidine-rich glycoprotein has no major function in serum heme transport. Nonetheless, the binding of heme by .alpha.2-histidine-rich glycoprotein provides a means of studying the structure of this protein using the heme chromophore as a probe. .alpha.2-Histidine-rich glycoprotein also binds other organic molecules including bilirubin, diaquocobinamide, Cibacron blue F3GA and rose bengal and certain divalent metals. It is of interest that Cu, Zn, Ni, Cd and Co effectively inhibit the binding of heme by .alpha.2-histidine-rich glycoproteins; other divalent metals tested, including Ca, Mg and Mn do not appreciably affect the heme-.alpha.2-histidine-rich glycoprotein interaction.

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