Literature DB >> 3686698

[A method of determining inhibitory constants during reversible inhibition of enzymatic hydrolysis of a substrate].

A P Brestkin, Iu G Zhukovskiĭ, E V Rozengart.   

Abstract

Determination of inhibitory constants and antienzymic activity of reversible retardants of different type of action by the generalized inhibitory constant K sigma is estimated, results being presented. To determine more precisely the values of inhibitory constants of the competitive (Ki), noncompetitive (K'i) inhibition and of the generalized K sigma it is suggested to conduct linearization of the experimental data in coordinates: 1/K sigma, s; 1/[S], where K sigma, s is a total inhibitory constant whose value depends on the substrate [S] concentration and to make calculations by the least-square method with the allowance for principal intervals of the Km values and the maximal rate of the enzymic reaction V. Comparative calculations are made by a computer using the BASIC/RT-60 language programme through the example of the acetyl choline acetyl hydrolase (EC 3.1.1.7) interaction with the quaternary phosphonium salts--reversible retardants of this enzyme.

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Year:  1987        PMID: 3686698

Source DB:  PubMed          Journal:  Ukr Biokhim Zh (1978)        ISSN: 0201-8470


  1 in total

1.  The effect of ionic strength on the reversible inhibition of acetylcholinesterase under the influence of thionephosphonates of different hydrophobicity.

Authors:  E V Rozengart; N E Basova
Journal:  Dokl Biochem Biophys       Date:  2006 Sep-Oct       Impact factor: 0.788

  1 in total

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