Further characterization of L-beta-hydroxyacid dehydrogenase from Drosophila.
Further characterization of L-beta-hydroxyacid dehydrogenase from Drosophila.
复制标题
果蝇 L-β-羟酸脱氢酶的进一步表征。
DOI：
10.1016/0304-4165(85)90269-7
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Sullivan,DT
中科院分区：
文献类型：
--
作者：
Menotti-Raymond,M;Sullivan,DT
L-β-Hydroxyacid dehydrogenase (L-β-hydroxyacid--NAD-oxidoreductase, EC 1.1.1.45) ofDrosophilais composed of two, identical subunits with a molecular weight of approx. 33 300. The enzyme was purified 938-fold fromDrosophila melanogaster. An isoelectric point of 8.6 was determined forL-β-hydroxyacid dehydrogenase. An amino acid analysis was conducted of the purified enzyme. A single subunit was obtained by SDS-gel electrophoresis of the purified enzyme. Translation of larval and adult mRNA in a mRNA-dependent reticulocyte lysate, followed by immune precipitation using anti-L-β-hydroxyacid dehydrogenase IgG revealed a singleL-β-hydroxyacid dehydrogenase subunit of 33 300. Larval and adult proteins were the same size. The enzyme does not appear to be subjected to substantial post-translational modifications.
