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6-Phosphogluconate dehydrogenase fromDrosophila melanogaster. I. Purification and properties of the a isozyme

✍ Scribed by John H. Williamson; Diane Krochko; Billy W. Geer

Publisher
Springer
Year
1980
Tongue
English
Weight
699 KB
Volume
18
Category
Article
ISSN
0006-2928

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✦ Synopsis

Drosophila melanogaster. The activity level is highest in early third instar larvae and declines to a lower, but relatively constant, level at all later stages of development. The enzyme is localized in the cytosolic portion of the cell. The A-isozymic form of 6-phosphogluconate dehydrogenase was purified to homogeneity and has a molecular weight of 105,000. The enzyme is a dimer consisting of subunits with molecular weights of 55,000 and 53,000. For the oxidative decarboxylation of 6-phosphogluconate the Kmfor substrate is 81/~M while that for NADP + is 22.3 ktM. The optimum pH for activity is 7.8 while the optimum temperature is 37 C.

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