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- W2021504965 abstract "Several barbiturates inhibit the degradation of enkephalin by the enzyme enkephalinase, a membrane-associated endopeptidase of rat striatum. The barbiturates vary largely in their inhibitory potential toward this enzymatic activity. Secobarbital, pentobarbital, phenobarbital and barbital inhibit the hydrolysis of Leu-enkephalin with IC50 of 8 × 10−6M, 1.8 × 10−5M, 7 × 10−5M and 4 × 10−4M, respectively. The N-1 methyl substituted barbiturates, methohexital and hexobarbital, as well as barbituric acid have very low or no inhibitory activity. The inhibition of Leu-enkephalin degradation by secobarbital exhibits mixed noncompetitive-competitive kinetics with KIS of 2 × 10−5M and KII of 6 × 10−5M. Solubilization of enkephalinase from the membranes with Triton X-100 does not effect the inhibition by the barbiturates. The barbiturates do not inhibit two other brain enzymes shown to degrade enkephalin, i.e. the enkephalin-degrading aminopeptidase and enkephalinase B. In addition, the hydrolysis of enkephalin by carboxypeptidase A or by thermolysin is not affected by the barbiturates." @default.
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- W2021504965 date "1981-01-01" @default.
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- W2021504965 title "The effect of barbiturates on the degradation of enkephalin by brain enzymes" @default.
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- W2021504965 doi "https://doi.org/10.1016/0024-3205(81)90551-8" @default.
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