Literature DB >> 3691807

Acetylcholinesterase as polyelectrolyte in reaction with cationic substrates.

V Tóugu1, A Pedak, T Kesvatera, A Aaviksaar.   

Abstract

It is shown that the salt effect in acetylcholinesterase-catalyzed hydrolysis of 2-(N-methylmorpholinium)-ethylacetate can be quantitatively described by the equation log(k2/KS) = log(k2/KS) degrees--psi log[M+Z] following from Manning's polyelectrolyte theory; the psi values for salts with univalent and bivalent cations at different pH values of the reaction medium were in accordance with the conclusions of the theory. Manning's polyelectrolyte theory seems to be a useful framework for studying salt effects in the reactions of charged substrates with enzymes as globular polyions.

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Year:  1987        PMID: 3691807     DOI: 10.1016/0014-5793(87)81134-1

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


  1 in total

1.  The active site and partial sequence of cobra venom acetylcholinesterase.

Authors:  C Weise; H J Kreienkamp; R Raba; A Aaviksaar; F Hucho
Journal:  J Protein Chem       Date:  1990-02
  1 in total

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