Abstract

When rats were treated with phenobarbital (PB), the activity of CBA reductase, which catalyzes the conversion of 2-carboxybenzaldehyde (CBA) to 2-hydroxymethylbenzoic acid (HMB), in the liver was markedly enhanced. Likewise, addition of PB to the primary culture of rat hepatocytes increased the activity of CBA reductase. The enzyme recovered from cell lysate of cultured cells showed the same characteristics in molecular and catalytic properties as the enzyme purified from the livers of the rats treated with PB. Experiments with cycloheximide suggest that de novo synthesis of the enzyme protein is enhanced by PB in primary culture.

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