A comparative study of carboxylesterase in the white mouse and in the caterpillar of the cotton bollworm Heliothes armigera

Studies have been made on enzymic hydrolysis of p-nitrophenylacetate (p-NPhAc), n-nitrophenylbutyrate (p-NPhBu) and indophenylacetate (IPhAc) by carboxylesterase (CE) from mouse blood plasma and liver as well as from caterpillar of the cotton worm haemolymph, intestine and fat body. Different KM and...

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Bibliographic Details
Published in:	Žurnal ėvolûtsionnoj biohimii i fiziologii Vol. 30; no. 5; p. 650
Main Authors:	Kugusheva, L I, Nesterov, V P, Rozengart, V I, Dorenskaia, G M, Kulieva, A M
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-09-1994
Subjects:	Animals Carboxylesterase Carboxylic Ester Hydrolases - metabolism Fat Body - enzymology Hemolymph - enzymology Hydrolysis Insecta - enzymology Intestines - enzymology Larva - enzymology Liver - enzymology Mice - metabolism Species Specificity Substrate Specificity
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Summary:	Studies have been made on enzymic hydrolysis of p-nitrophenylacetate (p-NPhAc), n-nitrophenylbutyrate (p-NPhBu) and indophenylacetate (IPhAc) by carboxylesterase (CE) from mouse blood plasma and liver as well as from caterpillar of the cotton worm haemolymph, intestine and fat body. Different KM and V max values were obtained for CE from these sources. The highest specific activity of CE from mouse liver and caterpillar intestine and fat body was observed with p-NPhBu. p-NPhAc is the best substrate for CE from mouse blood serum and caterpillar haemolymph. Carboxylesterases from mouse and caterpillar differed in their sensitivity to armine and paraoxone by 1-2 orders depending on the substrate used. Species and tissue differences in the kinetics of CE-catalyzed reactions with different substrates and inhibitors were revealed.
ISSN:	0044-4529