Abstract
The developmental kinetics of several amino acid and protein catabolizing enzymes have been studied. Aminopeptidase and alanine transaminase have been found to increase approximately 3-fold starting at the time of starvation and reaching maximum activity at 18 and 5 hours, respectively. The increase of both enzymes is sensitive to actinomycin D and cycloheximide, suggesting that prior RNA and concomitant protein synthesis are necessary for the increase. Neither enzyme increases in a mutant which does not aggregate. Aminopeptidase but not alanine transaminase shows temporal regulation in the temporally deranged mutants FR-17 and GN-3. This paper also confirms that glutamate dehydrogenase and lactate dehydrogenase, and aspartate transaminase are not developmentally regulated. Aminopeptidase and alanine transaminase appear to be a single molecular species.
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