Literature DB >> 7229264

Analysis of progress curves in enzyme kinetics: bias and convergent set in the differential and in the integral method.

M Markus, T Plesser, M Kohlmeier.   

Abstract

Two problems encountered in the analysis of progress curves are examined: 1. Systematic deviations due to errors in the initial solute concentrations make the least-squares method unsuitable. The improvements accomplished by the introduction of a proper weighting matrix are investigated. 2. Non-linear parameter optimization implies a dependence of the optimized parameters on their initial estimates, due to the existence of multiple minima. It is shown that the sensitivity of the optimized parameters on the initial estimates is reduced by fitting the slopes of the progress curves. A subsequent fit of the original progress curve data is recommended for refinement of the parameters.

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Year:  1981        PMID: 7229264     DOI: 10.1016/0165-022x(81)90021-x

Source DB:  PubMed          Journal:  J Biochem Biophys Methods        ISSN: 0165-022X


  3 in total

1.  Isothermal titration calorimetric study of RNase-A kinetics (cCMP --> 3'-CMP) involving end-product inhibition.

Authors:  Shawn D Spencer; Robert B Raffa
Journal:  Pharm Res       Date:  2004-09       Impact factor: 4.200

2.  A single-parameter family of adjustments for fitting enzyme kinetic models to progress-curve data.

Authors:  R G Duggleby; J C Nash
Journal:  Biochem J       Date:  1989-01-01       Impact factor: 3.857

3.  A novel parameter estimation from the linearized Michaelis-Menten equation at low substrate concentrations.

Authors:  T Keleti
Journal:  Biochem J       Date:  1982-04-01       Impact factor: 3.857

  3 in total

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