Reactivation of carboxylester hydrolase following inhibition by 4-nitrophenyl organophosphinates.
Biochem Pharmacol
; 34(10): 1789-94, 1985 May 15.
Article
en En
| MEDLINE
| ID: mdl-4004894
Porcine liver carboxylester hydrolase (EC 3.1.1.1; carboxylesterase) was rapidly inhibited by 4-nitrophenyl organophosphinates containing aryl or heteroaryl groups directly bound to phosphorus. The most potent inhibitor was 4-nitrophenyl di-2-thienylphosphinate for which the median inhibitory concentration was 7.4 X 10(-9) M. Rabbit liver monomeric carboxylester hydrolase was inhibited, separated from excess inhibitor by gel permeation chromatography, and observed for spontaneous or 1,1'-trimethylene-bis(4-formylpyridinium bromide) dioxime (TMB-4)-induced reactivation. Recovery was most rapid (k = 4 to 7 X 10(-4) min-1) from phosphinyl groups containing one alkyl substituent smaller than isopropyl and one aryl or heteroaryl group smaller than naphthyl. The di-2-thienylphosphinylated enzyme was an exception since it recovered rapidly while lacking an alkyl substituent. Oxime reactivation by TMB-4 doubled rates of recovery.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ácidos Fosfínicos
/
Hidrolasas de Éster Carboxílico
/
Reactivadores Enzimáticos
Límite:
Animals
Idioma:
En
Revista:
Biochem Pharmacol
Año:
1985
Tipo del documento:
Article
Pais de publicación:
Reino Unido