[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 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.
Kugusheva
L I
LI
Nesterov
V P
VP
Rozengart
V I
VI
Dorenskaia
G M
GM
Kulieva
A M
AM
D000818:Animals; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D005216:Fat Body / Q000201:enzymology; D006458:Hemolymph / Q000201:enzymology; D006868:Hydrolysis; D007313:Insecta / Q000201:enzymology*; D007422:Intestines / Q000201:enzymology; D007814:Larva / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D051379:Mice / Q000378:metabolism*; D013045:Species Specificity; D013379:Substrate Specificity
D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase
Sravnitel'noe issledovanie karboksilésterazy beloĭ myshi i gusenitsy khlopkovoĭ sovki Heliothis armigera.