Abstract
MenNC1was isolated from a wild-type population as a putative NADP-Malic enzyme null-activity mutant. Detailed analysis of this mutant revealed that MenNC1homozygotes exhibit 3 to 5% of normal levels of NADP-ME activity throughout development. NADP-ME purified from MenNC1homozygotes is not different from NADP-ME purified from a standard wild-type strain when electrophoretic mobility, molecular weight, substrate kinetics and temperature optima are compared. Quantitative rocket immunoelectrophoresis has demonstrated reduction of NADP-ME-specific protein in MenNC1homozygotes proportionate to activity levels. It is suggested that MenNC1may represent a regulatory locus controlling levels of NADP-ME in Drosophila.
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