Literature DB >> 4077467

Acetylcholinesterase inhibition by eserine: rate constants of reaction. Part II.

M Brufani, S Lippa, M Marta, A Oradei, M Pomponi.   

Abstract

The inhibition of eel acetylcholinesterase by physostigmine at 20 degrees and 25 degrees C have been investigated. In our evaluation the unimolecular reactivation rate constant, k3, the carbamylation rate constant, k2, and the binding constant, Ka, are the first simultaneously determined. The mechanism of this reaction is discussed.

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Year:  1985        PMID: 4077467

Source DB:  PubMed          Journal:  Ital J Biochem        ISSN: 0021-2938


  2 in total

1.  Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis.

Authors:  Terrone L Rosenberry; Leilani K Sonoda; Sarah E Dekat; Bernadette Cusack; Joseph L Johnson
Journal:  Chem Biol Interact       Date:  2008-06-17       Impact factor: 5.192

2.  Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter.

Authors:  Terrone L Rosenberry; Leilani K Sonoda; Sarah E Dekat; Bernadette Cusack; Joseph L Johnson
Journal:  Biochemistry       Date:  2008-12-09       Impact factor: 3.162

  2 in total

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