Binding of Human Hemoglobin and Its Polypeptide Chains with Haptoglobin Coupled to an Agarose Matrix
- 1 May 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 64 (2) , 369-372
- https://doi.org/10.1111/j.1432-1033.1976.tb10310.x
Abstract
The interactions of human haptoglobin covalently linked to agarose with human Hb and with p-chloromercuribenzoic-acid-treated .alpha. and .beta. chains (.alpha.* and .beta.* chains) were studied by flow chromatography and equilibrium binding. In solid state, haptoglobin maintained the same binding characteristics as in solution, the order of binding affinities being: Hb < .alpha.* chain < .beta.* chain. The study of the binding parameters of the .alpha.* chain showed an heterogeneity of binding sites on the haptoglobin and an average affinity constant Ka of 3.6 .times. 104 l/mol.This publication has 38 references indexed in Scilit:
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