文摘
This work presents an alternative analysis of the integrated rate equations corresponding to the simple Michaelis-Menten mechanism without product inhibition. The suggested new results are reached under a minimal set of assumptions and include, as a particular case, the classical integrated Michaelis–Menten equation. Experimental designs and a kinetic data analysis are suggested to the estimation of the maximum steady-state rate, V max, the Michaelis–Menten constant, K m, the initial enzyme concentration, [E]0, and the catalytic constant, k 2. The goodness of the analysis is tested with simulated time progress curves obtained by numerical integration.