Abstract
Glutamine synthetase prepared from internal tissues of Prodenia eridania larvae was purified about 4-fold by isoelectric precipitation of acetone-powder extracs. The relatively unstable enzyme incubated with l-glutamate, NH 4 + (orNH 2OH), ATP and Mg 2+ formed stoichiometric amounts of glutamine (or γ-glutamylhydroxamate), ADP and inorganic phosphate. The hydroxamate reaction with d-glutamate was considerably slower than with the l-isomer. γ-Glutamyl-transferase activity was about three times that of the synthetase. Characterization of the insect enzyme did not reveal any special or unique properties. Synthetase activity was highest in the larval fat-body, the gut and Malpighian tubules had a much lower titer, and little or no activity was found in the hemolymph. During adult development a more or less progressive decrease in synthetase activity occurred until just before emergence of the adult moth when the titer increased slightly.
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