Binding of human hemoglobin and its polypeptide chains with haptoglobin coupled to an agarose matrix.
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.
D001665:Binding Sites; D002729:Chloromercuribenzoates; D006242:Haptoglobins; D006454:Hemoglobins; D006801:Humans; D007700:Kinetics; D008024:Ligands; D046911:Macromolecular Substances; D008433:Mathematics; D011485:Protein Binding; D011487:Protein Conformation; D012685:Sepharose
D002729:Chloromercuribenzoates; D006242:Haptoglobins; D006454:Hemoglobins; D008024:Ligands; D046911:Macromolecular Substances; D012685:Sepharose