Abstract
Glutamine-dependent carbamylphosphate synthetase, aspartate transcarbamylase, and dihydroorotase cosediment as a high-molecular-weight complex in Drosophila embryos and pupae. Although the larval enzyme is very labile, we show that the same high-molecular-weight polypeptide can be isolated by immunological methods from larvae as already described for cultured embryonic cells. However, the greater sensitivity of the larval enzyme to proteolysis when compared to the enzyme from embryos and the biochemical analysis of a cold-sensitive lethal allele of rudimentary, the structural gene for this polypeptide, strongly indicates that conformational changes occur within the complex in the course of development.
Published Version
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