A kinetic analysis is presented of reactions of protein modification, and/or of modification-induced enzyme inactivation, which can formally be described by a single exponential function, or by a summation of two exponential functions, of reaction time plus a constant term. The reaction schemes compatible with the kinetic formalism of these cases are given, and a simple kinetic criterion is described whereby the identification of one of these cases, strong negative protein modification co-operativity, may be carried out. The treatment outlined in this paper is applied to a case from the literature, the inactivation of glyceraldehyde-3-phosphate dehydrogenase by butane-2,3-dione [Asriyants, Benkevich & Nagradova (1983) Biokhimiya (Engl. Transl.) 48, 164-171].
Research Article|November 01 1989
Kinetic analysis of protein modification reactions at equilibrium
Biochem J (1989) 263 (3): 855-859.
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E T Rakitzis; Kinetic analysis of protein modification reactions at equilibrium. Biochem J 1 November 1989; 263 (3): 855–859. doi: https://doi.org/10.1042/bj2630855
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