Phosphopyruvate carboxylase induction by L-tryptophan. Effects on synthesis and degradation of the enzyme.
1. The administration of l-tryptophan to fed rats produces a twofold increase in hepatic phosphopyruvate carboxylase activity that represents a comparable increase in enzyme protein. With specific antibody against the enzyme we have shown that the increase in phosphopyruvate carboxylase is partially mediated via an actinomycin D-sensitive increase in enzyme synthesis. 2. In starved animals tryptophan increases the enzyme activity without any change in the relative rate of phosphopyruvate carboxylase synthesis. In this condition degradation of the enzyme is retarded by tryptophan by a mechanism that is not prevented by cycloheximide.
D000818:Animals; D000936:Antigen-Antibody Complex; D003513:Cycloheximide / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D003609:Dactinomycin; D007930:Leucine / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D008297:Male; D009929:Organ Size; D010729:Phosphoenolpyruvate Carboxykinase (GTP) / Q000378:metabolism*; D051381:Rats; D013217:Starvation; D014316:Tritium; D014364:Tryptophan / Q000494:pharmacology*
D000936:Antigen-Antibody Complex; D014316:Tritium; D003609:Dactinomycin; D014364:Tryptophan; D003513:Cycloheximide; D010729:Phosphoenolpyruvate Carboxykinase (GTP); D007930:Leucine