Purification and properties of wild-type and mutant glucose 6-phosphate dehydrogenases and of 6-phosphogluconate dehydrogenase from Drosophila melanogaster.
スポンサーリンク
概要
- 論文の詳細を見る
Glucose 6-phosphate dehydrogenase was purified to a homogeneous state from Drosophila melanogaster imagoes made homozygous for the X chromosome of a mutant male which showed two bands of enzyme activity on polyacrylamide gels as well as from Oregon R flies similarly made homozygous which showed only one major band, and their properties were compared with respect to molecular weight, pH optimum, specific activity, Km values and sensitivity to p-chloromercuribenzoate, MgCl2, dehydroepiandrosterone, heat and anti-Oregon R glucose 6-phosphate dehydrogenase antibody.The fast and slow bands of mutant enzyme had molecular weights of 115, 000 and 283, 000, respectively, while the wild-type enzyme had a molecular weight of 120, 000. Treatment with sodium dodecyl sulfate cleaved the three enzymes into a subunit having a molecular weight of 69, 000. This suggests that the slow and fast bands of the mutant enzyme represent tetramers and dimers of single polypeptides, respectively. Since the mobility of the fast mutant enzyme was the same as that of wild-type enzyme, it is inferred that the mutation resulted in a change of the quaternary structure of enzyme, without affecting its net charge in this particular instance. The mutant enzyme was more heat-stable than the wild-type enzyme, but they did not differ in other respects.6-Phosphogluconate dehydrogenase was also purified to a homogeneous state from the wild and mutant flies. No difference was found between the two strains of flies with respect to several parameters used.
- 日本遺伝学会の論文
日本遺伝学会 | 論文
- キイロショウジョウバエにおけるP因子の切り出し頻度と転移頻度の独立性〔英文〕
- ショウジョウバエ筋突然変異wings-up Bの電子顕微鏡および電気泳動法による解析〔英文〕
- 組み合わせ染色体処理と画像法による姉妹染色分体交換位置の同定
- 日本産ハツカネズミ集団における蛋白質変異の地理的分布〔英文〕
- 日本産ハツカネズミのId-1遺伝子座に観察された第3の遺伝子,Id-C,の分布と起源〔英文〕