1. In an enzyme that has two independent binding sites for a ligand, any inhibitor that binds solely to the free enzyme will give rise to positive co-operativity. 2. A model is considered for the allosteric control of enzymes by effectors in which their effects are mediated by ligand-induced perturbations of the ionization constants of a group or groups involved in the binding of substrate to the active site. 3. The model described offers a plausible explanation for the observation that the sigmoidal initial-rate curves reported for some regulatory enzymes are not expressed at all pH values where the enzyme is catalytically active.
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Research Article| November 01 1977
A model for the allosteric regulation of pH-sensitive enzymes
Biochem J (1977) 167 (2): 479–482.
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J S Shindler, K F Tipton; A model for the allosteric regulation of pH-sensitive enzymes. Biochem J 1 November 1977; 167 (2): 479–482. doi: https://doi.org/10.1042/bj1670479
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