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The functional relationship between polymerization and catalytic activity of beef liver glutamate dehydrogenase. I. Theory


The functional relationship between polymerization and catalytic activity of beef liver glutamate dehydrogenase. I. Theory



Journal of Molecular Biology 108(1): 151-178



ISSN/ISBN: 0022-2836

PMID: 1003482

DOI: 10.1016/s0022-2836(76)80101-5

The reversible polymerization of beef liver glutamate dehydrogenase may play an important role in the allosteric control of this enzyme. A simple quantitative model for analyzing the detailed relationship between the distribution of enzyme polymers and the catalytic activity of the enzyme solution was presented. The model was tested using quasi-elastic light-scattering spectroscopic determinations of polymer distribution and biochemical determinations of enzyme activity. In this paper the mathematical development of the original model is completed. Subsequent more extensive experimental investigations have led to a modification of the original model to obtain even closer agreement between theory and experiment. Hence 2 alternative versions of the model are presented. The original model presumed that the enzyme polymers must be homogenous, in that all of the constituents of a given polymer had to be in the same conformational state. The 2 alternative models deal explicitly with the possibility of forming polymers composed of elements in different conformational states. The theoretical framework necessary to relate the distribution of polymers predicted by any of the 3 models with the distribution of diffusion constants measured by quasi-elastic light-scattering spectroscopy is developed.

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Accession: 068539746

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Related references

Does a functional relationship exist between the polymerization and catalytic activity of beef liver glutamate dehydrogenase?. Journal of Molecular Biology 115(2): 243-247, 1977

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