Literature DB >> 20253

New enzymatic assay of cholinesterase activity.

H Okabe, K Sagesaka, N Nakajima, A Noma.   

Abstract

A new enzymatic method for the determination of serum pseudo-cholinesterase activity is described. Choline, which is liberated from benzoylcholine as substrate by cholinesterase, is oxidized by choline oxidase to betaine with the simultaneous production of hydrogen peroxide, which oxidatively couples with 4-aminoantipyrine and phenol in the presence of peroxidase to yield a chromogen with maximal absorbance at 500 nm. The calibration curve is linear up to 1500 units per liter of serum. The method is reproducible, and the results correlate well with those obtained by the method using butyrylthiocholine as substrate and 5,5'-dithiobis-(2-nitrobenzoic acid) as color reagent.

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Year:  1977        PMID: 20253     DOI: 10.1016/0009-8981(77)90267-4

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  2 in total

1.  Biological monitoring of human exposure to acephate.

Authors:  M Maroni; G Catenacci; D Galli; D Cavallo; G Ravazzani
Journal:  Arch Environ Contam Toxicol       Date:  1990 Sep-Oct       Impact factor: 2.804

Review 2.  Assessment of Enzyme Inhibition: A Review with Examples from the Development of Monoamine Oxidase and Cholinesterase Inhibitory Drugs.

Authors:  Rona R Ramsay; Keith F Tipton
Journal:  Molecules       Date:  2017-07-15       Impact factor: 4.411

  2 in total

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