| Autor: |
L I, Kugusheva, V P, Nesterov, V I, Rozengart, G M, Dorenskaia, A M, Kulieva |
| Rok vydání: |
1994 |
| Předmět: |
|
| Zdroj: |
Zhurnal evoliutsionnoi biokhimii i fiziologii. 30(5) |
| ISSN: |
0044-4529 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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