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Dissociation of Oxyhaemoglobin, Methaemoglobin and their Hybrid compared by Difference Gel Chromatography

Nature New Biology volume 235, pages 110–112 (1972)Cite this article

Abstract

ACCURATE measurement of the energy of protein subunit interaction1–7 is an essential step in the study of cooperative and allosteric8–10 effects in proteins. It is, however, more often the change of this energy on uptake of ligand or substrate which is the more important quantity to be determined, not its total value. Likewise it is the variation of interaction energy from protein to protein which is of more interest when phylogenetically related proteins are compared, and again it is differences in energy of combination which determine how much hybrid is formed when closely related reversibly dissociating proteins are present in mixture in solution.

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Authors and Affiliations

  1. Department of Biochemistry, University of Birmingham,

    G. A. GILBERT, LILO M. GILBERT, CHRISTINE E. OWENS & NAHED A. F. SHAWKY

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  1. G. A. GILBERT
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  2. LILO M. GILBERT
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  3. CHRISTINE E. OWENS
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  4. NAHED A. F. SHAWKY
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GILBERT, G., GILBERT, L., OWENS, C. et al. Dissociation of Oxyhaemoglobin, Methaemoglobin and their Hybrid compared by Difference Gel Chromatography. Nature New Biology 235, 110–112 (1972). https://doi.org/10.1038/newbio235110a0

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