beta-Galactosidase is induced by hormone in Drosophila melanogaster cell cultures.

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Abstract
D. melanogaster cell lines Kc and Ca and clones FC and RF6, cultured in vitro, have no detectable .beta.-galactosidase (.beta.-D-galactoside galactohydrolase, EC 3.2.1.23) activity (as measured by hydrolysis of o-nitrophenyl-.beta.-D-galactoside). Ecdysterone clearly induces .beta.-galactosidase activity in D. melanogaster cells cultured in vitro. Induction occurs in cell lines or clones sensitive to ecdysterone (K, Ca, and Fc) and does not occur in clones resistant to the hormone (RF6). Some properties of the hormone-induced .beta.-galactosidase activity were studied. The Km for o-nitrophenyl galactoside is 0.35 mM and the Ki for lactose is 12 mM (similar to those of Escherichia coli .beta.-galactosidase); the activity can be recovered after sodium dodecyl sulfate treatment; the enzyme is a tetramer (Mr [molecular ratio] of the monomer is 64,000).