[Comparative sensitivity of 2 carboxylesterases from the reindeer liver to various inhibitors]. / Sravnitel'naia chuvstvitel'nost' dvukh karboksilésteraz iz pecheni severnogo olenia k nekotorym ingibitoram.
Biokhimiia
; 51(7): 1141-9, 1986 Jul.
Article
em Ru
| MEDLINE
| ID: mdl-3730448
ABSTRACT
The sensitivity to the inhibitor of two forms of reindeer liver carboxylesterases differing in electrophoretic mobility and conventionally termed as "slow" and "fast" forms were investigated. The rate constants for the interaction of organophosphorous irreversible inhibitors--diisopropylfluorophosphate (DPP) and two methylthiophosphonic acid thioesters--C5H11O(CH3)P(O)S(CH2)SCH2C(O)OCH3 (Sh-205) and, C8H17O(CH3)P(O)S(CH2)SCH2C(O)OCH2 (Sh-207)--with the "fast" form are hundreds of times as high as those with the "slow" one. The rate constants for irreversible carbamate inhibitor interaction byehone with both carboxylesterase forms were approximately equal to 1.2 X 10(3) M-1 X min-1 and 2.0 X 10(3) M-1 X min-1, respectively. The reversible inhibitors potassium benzylate and kathapin also inhibited the "fast" carboxylesterase form in the indophenylacetate (IPA) hydrolysis reaction (770 and 1700-fold, respectively). On the contrary, N-methylpiperidinyl ester of benzyl acid inhibited the "slow" form three times stronger. Carbophos reversibly inhibited IPA hydrolysis in the presence of both enzyme forms, but the carboxyester carbophos group was hydrolyzed at a measurable speed only by the "slow" form.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hidrolases de Éster Carboxílico
/
Fígado
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
Ru
Revista:
Biokhimiia
Ano de publicação:
1986
Tipo de documento:
Article
País de publicação:
FEDERAÇÃO RUSSA
/
RU
/
RUSIA
/
RUSSIA