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...

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Bibliographic Details
Published in:Biochemical journal 1973-10, Vol.136 (2), p.259-264
Main Authors: Ballard, F J, Hopgood, M F
Format: Article
Language:English
Subjects:
Animals
Antigen-Antibody Complex
Cellular Interactions and Control Processes
Cycloheximide - pharmacology
Cytosol - enzymology
Dactinomycin
Leucine - metabolism
Liver - enzymology
Male
Organ Size
Phosphoenolpyruvate Carboxykinase (GTP) - metabolism
Rats
Starvation
Tritium
Tryptophan - pharmacology
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Summary: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.
ISSN:0264-6021
0306-3283
1470-8728
DOI:10.1042/bj1360259