Properties of choline acetyltransferase from the bulb miteRhizoglyphus echinopus (Acari: Acaridae)

Autor:	Charles O. Knowles, Daniel D. Errampalli
Rok vydání:	1991
Předmět:	chemistry.chemical_classification Ecology biology Thiazolidine General Medicine biology.organism_classification Choline acetyltransferase Bulb chemistry.chemical_compound Enzyme chemistry Biochemistry Animal ecology Insect Science medicine Choline Acaridae Acetylcholine medicine.drug
Zdroj:	Experimental & Applied Acarology. 12:119-128
ISSN:	1572-9702 0168-8162
DOI:	10.1007/bf01204405
Popis:	In the presence of exogenous acetyl coenzyme A14-C and choline, the 20 000 g supernatant fraction of whole bulb-mite homogenates synthesized a radioactive product that chromatographed with authentic acetylcholine (ACh). ApparentKm values were 0.12 and 1.14 mM for acetyl coenzyme A and choline, respectively, and the average rate of ACh synthesis was 2.06 μmol h−1 g−1 equivalent of mite tissue (wet weight). Choline acetyltransferase (ChAT) activity was inhibited by 5,5′-dithiobis(2-nitrobenzoic acid), suggesting the presence of functionally important sulfhydryl groups. However, ChAT activity was not inhibited by 27 acaricides from several different chemical classes, except for the thiazolidine flubenzimine which gave a pI50 of 3.5 mol l−1.
Databáze:	OpenAIRE
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