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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Mar;75(3):1101–1105. doi: 10.1073/pnas.75.3.1101

Unsymmetrical and concerted examples of the effect of enzyme--enzyme interactions on steady-state enzyme kinetics.

T L Hill
PMCID: PMC411416  PMID: 274700

Abstract

In previous papers of this series, emphasis has been placed on the steady-state phase transition and critical properties of large lattices of interacting, symmetrical, and identical enzyme molecules. The present paper is concerned with a number of examples of enzyme--enzyme interactions that do not belong to the class of models of the earlier papers. These are more biochemically oriented and include heterologous dimers, a linear chain with unsymmetrical interactions, and concerted isologous dimers (half-the-sites reactivity).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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