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  • Title: Binding of human hemoglobin and its polypeptide chains with haptoglobin coupled to an agarose matrix.
    Author: Tsapis A, Rogard M, Alfsen A, Mihaesco C.
    Journal: Eur J Biochem; 1976 May 01; 64(2):369-72. PubMed ID: 1278164.
    Abstract:
    The interactions of human haptoglobin covalently linked to agarose with human hemoglobin and with p-chloromercuribenzoic-acid-treated alpha and beta chains (alpha* and beta* chains) were studied by flow chromatography and equilibrium binding. The results indicate that in solid state, haptoglobin maintains the same binding characteristics as in solution, the order of binding affinities being: hemoglobin greater than alpha* chain greater than beta* chain. The study of the binding parameters of the alpha* chain shows an heterogeneity of binding sites on the haptoglobin and an average affinity constant Ka of 3.6 X 10(4)l/mol.
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