Literature DB >> 9276440

A simple method for determining kinetic constants of complexing inactivation at identical enzyme and inhibitor concentrations.

M H Wang1, K Y Zhao.   

Abstract

The kinetics of complexing inactivation at identical enzyme and inhibitor concentrations were analyzed and the equations of product generation were derived when the free enzyme concentration is great, larger or smaller than the dissociation constant of inhibitor, K(I). The kinetic constants can be obtained by fitting the derived equations to the progress curve. Numerical examples show that this method is valid and gives satisfactory results.

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Year:  1997        PMID: 9276440     DOI: 10.1016/s0014-5793(97)00771-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Primer release is the rate-limiting event in lagging-strand synthesis mediated by the T7 replisome.

Authors:  Alfredo J Hernandez; Seung-Joo Lee; Charles C Richardson
Journal:  Proc Natl Acad Sci U S A       Date:  2016-05-09       Impact factor: 11.205

2.  Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins.

Authors:  Alfredo J Hernandez; Charles C Richardson
Journal:  J Vis Exp       Date:  2017-02-25       Impact factor: 1.355

  2 in total

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