Purification and partial characterization of alcohol dehydrogenase, fructose-1,6-bisphosphate aldolase and the cytoplasmic form of malate dehydrogenase from Drosophila melanogaster
Abstract
A purification scheme for the cytoplasmic form of malate dehydrogenase (s-MDH) of Drosophila melanogaster is presented which is superior to any previously reported method. In addition, this scheme can also be used to obtain alcohol dehydrogenase (ADH) and FDP aldolase. Gel filtration experiments reveal an oligomeric molecular weight of 69,000 for s-MDH, and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate indicates subunit molcular weights of 32,100 for s-MDH, 24,600 for ADH and 34,000 for FDP aldolase. The amino acid composition of Drosophila melanogaster s-MDH and FDP aldolase are reported. © 1984.
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