Abstract
Recently a great deal of attention has been focused on subunit interactions in polymeric enzymes. Following Adair’s original discovery of cooperative 02 binding in hemoglobin (1), a large and growing list of proteins have been found to exhibit some type of subunit interaction (2,3). Several very elegant models have been pronosed to explain these effects but it now appears that no one model can adequately describe all of the varied behavior observed.
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MacQuarrie, R.A., Bernhard, S.A. (1970). On the Relationship between Protein Conformation and Enzyme-Substrate Covalent Bond Formation in Glyceraldehyde-3-Phosphate Dehydrogenase. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_16
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DOI: https://doi.org/10.1007/978-3-642-49974-6_16
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