Abstract
Descriptions are given for the graphical determination of molecular pK values from the curves of logV and p(Km/V) against pH. The arguments are based on the model dissociation equilibria LAL in equilibrium (AL + LA) in equilibrium A, where A denotes a molecule having two binding sites for a ligand L.
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Selected References
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- ALBERTY R. A., MASSEY V. On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction. Biochim Biophys Acta. 1954 Mar;13(3):347–353. doi: 10.1016/0006-3002(54)90340-6. [DOI] [PubMed] [Google Scholar]
- Brocklehurst K., Dixon H. B. PH-dependence of the steady-state rate of a two-step enzymic reaction. Biochem J. 1976 Apr 1;155(1):61–70. doi: 10.1042/bj1550061. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dixon H. B., Tipton K. F. Negatively co-operative ligand binding. Biochem J. 1973 Aug;133(4):837–842. doi: 10.1042/bj1330837. [DOI] [PMC free article] [PubMed] [Google Scholar]