Sensitivity of Carboxylesterases of Rat Serum to Diethyl-p-nitrophenyl Phosphate

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Abstract
The effects of varying concentrations of the organophosphorus inhibitor E600 (diethyl-p-nitrophenyl phosphate) have been studied on the hydrolysis of a homologous series of n-alkyl aliphatic esters of α-naphthol by carboxylesterases of whole rat serum and by an esterase isozyme purified from the latter. The results indicate a regressing organophosphate susceptibility of the isozyme with progressively higher substrates. Inhibitor profiles of the whole serum, however, are more complex and do not exhibit any definite pattern in response to a sequential variation in the acyl carbon chain length of the esters. Both the isozyme and whole serum manifest an unusually high degree of organophosphate sensitivity towards substrates bearing odd number of carbon atoms in the acyl chain.