Abstract
The paper deals with interactions of substances via an enzymatic reaction (Bull. Math. Biophysics,25, 141–154, 1963). The substances are the activators, inhibitors and/or substrates of the reaction. Due to the bimolecularity of the processes in the reaction, the quantitative relation between the steady state amount of complexes and the amounts of the substances assumes a typical form. In multiple enzymatic reactions this form is more complicated, though basically similar. Because the substances may influence the steady state amounts of the complexes in opposite directions, the compensation and blocking effects are the properties of enzymatic reactions. The substances with the same direction of influence may potentiate each other. In the enzymatic reaction here considered, the potentiation is always non-negative.
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Literature
Landahl, H. D. 1958. “Theoretical Considerations on Potentiation in Drug Interaction.”Bull. Math. Biophysics,20, 1–23.
Ličko, V. 1963. “Some Notes on the Theory of Reaction Rates: Enzymatic Reactions.Bull. Math. Biophysics,25, 141–154.
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Ličko, V. Interactions in enzymatic reactions. Bulletin of Mathematical Biophysics 28, 379–390 (1966). https://doi.org/10.1007/BF02476820
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DOI: https://doi.org/10.1007/BF02476820