Literature DB >> 2742133

A general pre-steady-state solution to complex kinetic mechanisms.

X Z Zhang1, A Strand, H D White.   

Abstract

We have developed a general method for solving transient kinetic equations using Laplace transforms. Laplace transforms can be used to transform systems of differential equations that describe pre-steady-state kinetics to systems of linear algebraic equations. The general form of the pre-steady-state solution is (formula; see text) where I(t) is the time dependence of the physically observed property of the system, n is the number of intermediates, lambda i are the observed rate constants (reciprocals of the relaxation times), t is time, and Ii are the amplitude coefficients associated with each observed rate constant. We have written a program in compiled BASIC to run on a personal computer to evaluate Ii and lambda i. The program will evaluate the rate constants and coefficients of a mechanism with eight intermediates and seven relaxation times in 4 s on an 8-MHz PC-XT equipped with a math coprocessor. The most complex mechanism that we have solved, a mechanism containing 20 intermediates and 19 relaxation times, required approximately 5 min. We believe that this method will be useful to evaluate the differences in transient properties of complex biochemical mechanisms.

Mesh:

Year:  1989        PMID: 2742133     DOI: 10.1016/0003-2697(89)90336-9

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  5 in total

1.  Computer program for the expression of the kinetic equations of enzyme reactions as functions of the rate constants and the initial concentrations.

Authors:  R Varón; B H Havsteen; M García; F García Cánovas; J Tudela
Journal:  Biochem J       Date:  1990-09-15       Impact factor: 3.857

2.  Bovine inositol monophosphatase: enzyme-metal-ion interactions studied by pre-equilibrium fluorescence spectroscopy.

Authors:  M R Thorne; P J Greasley; M G Gore
Journal:  Biochem J       Date:  1996-05-01       Impact factor: 3.857

3.  Effects of K+ on the binding of Ca2+ to the Ca(2+)-ATPase of sarcoplasmic reticulum.

Authors:  A G Lee; K Baker; Y M Khan; J M East
Journal:  Biochem J       Date:  1995-01-01       Impact factor: 3.857

4.  Binding of Ca2+ to the (Ca(2+)-Mg2+)-ATPase of sarcoplasmic reticulum: kinetic studies.

Authors:  I M Henderson; A P Starling; M Wictome; J M East; A G Lee
Journal:  Biochem J       Date:  1994-02-01       Impact factor: 3.857

5.  Effects of polycations on Ca2+ binding to the Ca(2+)-ATPase.

Authors:  G Hughes; Y M Khan; J M East; A G Lee
Journal:  Biochem J       Date:  1995-06-01       Impact factor: 3.857

  5 in total

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