A method described previously [Cornish-Bowden & Endrenyi (1981) Biochem. J. 193, 1005-1008] for fitting theoretical equations to enzyme kinetic data without prior knowledge of weights or error distribution has been tested by computer simulation. With the equations for various kinds of linear inhibition as an example, the method performed well under all of the conditions examined, giving results that were often much better than those given by widely used least-squares alternatives, and were never appreciably worse. Although equations for two-substrate kinetics were not explicitly tested, the results for inhibition equations can be generalized to include two-substrate equations because the two are formally equivalent for simulation purposes. As a check on the results with inhibition equations the method was also tested for fitting bell-shaped pH-activity profiles and gave correspondingly good results.

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