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- W2007392308 abstract "Abstract The functional centre of haemoproteins is generally formed by an iron porphyrin and amino acid residues of he protein component. Some haemoproteins are able to bind imidazole to the iron of the prosthetic group. The synthesis of imidazole containing matrices is described and the affinity of haemoglobin as a model compound to these matrices has been studied. It was found that the lenght and structure of spacers as well as substituents at the imidazole ring are of critical importance: the adsorption of methaemoglobin shows two different kinds of protein matrix interaction: in case of a space length 5 A adsorption takes place via complex formation between imidazole and iron of a prosthetic group independent of the linkage in 1- or 4(5)-position of the imidazole ring to the mtrix: the complex formation between imidazole and iron is the decisive step but is not solely responsible for the stability of the ocmplex: a hydroxyl group at the side chain near the imidazole decreases the adsorption drastically: large substituents at the imidazole ring disturb complex formation with the iron, but not the adsorption of haemoglobin; in the presence of a long spacer (> 20 A), hydrophobic interactions are predominantly responsible for the adsorption process and imidazole does not play any role." @default.
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- W2007392308 date "1979-06-01" @default.
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- W2007392308 title "Affinity chromatography of haemoproteins: 1. Synthesis of various imidazole containing matrices and their interaction with haemoglobin" @default.
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- W2007392308 doi "https://doi.org/10.1016/0141-8130(79)90037-0" @default.
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