The α-glycerophosphate cycle inDrosophila melanogaster. I. Biochemical and developmental aspects
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- O'Brien, S.J. & MacIntyre, R.J. Biochem Genet (1972) 7: 141. doi:10.1007/BF00486085
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The two α-glycerophosphate dehydrogenases ofDrosophila melanogaster (mitochondrial αGPO and soluble αGPDH) have been biochemically characterized in a preliminary investigation of the α-glycerophosphate cycle inDrosophila. The soluble enzyme is NAD linked and can be distinguished from the mitochondrial oxidase in terms of locational specificity,pH optimum, salt precipitation, and electrophoretic behavior. The mitochondrial enzyme is NAD independent and exhibits behavior typical of a lipoprotein. Extraction procedures are described for αGPO with nonionic detergents. Isoelectric focusing of αGPO on polyacrylamide gels resolved two molecular forms of αGPO which differ in isoelectric point, ease of extraction, and developmental and spatial distribution. Developmental profiles of both αGPO and αGPDH are presented. The occurrence of multiple forms of both the soluble (Wright and Shaw, 1969) and the mitochondrial forms of the enzymes is discussed in light of a multifunctional role of the α-glycerophosphate cycle inDrosophila.