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• W1566128308 abstract "Abstract The regulation of N-acetyl-l-glutamate-dependent carbamyl phosphate synthetase (CP-synthetase) in vitro was studied using a suspension of surviving liver cubes prepared from Rana catesbeiana tadpoles and frogs. An enhancement of CP-synthetase activity was seen in preparations from premetamorphic tadpoles after incubation in vitro with l-thyroxine (2.6 x 10-8 or 2.6 x 10-9 m). Other additives, including a number of hormones, cyclic 3',5'-AMP, tadpole serum, and frog serum had no effect in vitro. Thyroxine added in vitro stimulated the rate of CP-synthetase synthesis in liver preparations from the premetamorphic and metamorphosing tadpoles and the frog. CP-synthetase synthesis in liver cubes was enhanced relative to soluble mitochondrial protein synthesis at thyroxine concentrations of 2.6 x 10-8 m and 2.6 x 10-9 m, and in liver cubes from both tadpoles previously treated with thiouracil and from tadpoles previously treated by immersion in thyroxine 2.6 x 10-7 m. Actinomycin D and puromycin added in vitro at zero time inhibited synthesis of CP-synthetase de novo. When liver cubes from tadpoles pulsed with leucine-3H in vivo were incubated in cold leucine in vitro, an increase in labeled immunoprecipitable CP-synthetase was observed in the presence of actinomycin or puromycin, suggesting an effect on the conversion of nonimmunoprecipitable precursors to labeled immunoprecipitable enzyme. The mechanism underlying the observed increase in conversion of precursors was shown to be caused by an inhibition of CP-synthetase turnover by puromycin and actinomycin. Thyroxine added in vitro resulted in an increase in precursor conversion. The small contribution of synthesis in vitro to the total CP-synthetase pool de novo suggested that enhancement of CP-synthetase levels in vitro was related largely to conversion of precursors to immunoprecipitable enzyme. This concept is consistent with the observation of an increase in total enzyme levels when liver cubes were incubated in the presence of actinomycin or puromycin. The regulation of CP-synthetase levels in liver preparations from the premetamorphic and metamorphosing tadpole, as well as the adult frog, appeared to be similar, and to involve a combination of CP-synthetase synthesis, precursor conversion, and degradation. The lag phase observed during induction of CP-synthetase synthesis and activity during thyroxine immersion in vivo was not observed in the liver cube preparations, suggesting the possibility of a repressor mechanism in vivo that was not operative in vitro. The nature of the repressor (or repressors) remains unknown." @default.
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• W1566128308 date "1969-10-01" @default.
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• W1566128308 title "Synthesis of Carbamyl Phosphate Synthetase in Amphibian Liver in Vitro" @default.
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• W1566128308 doi "https://doi.org/10.1016/s0021-9258(18)63660-9" @default.
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