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对斯氏艾美球虫(原生动物)中葡萄糖6-磷酸脱氢酶特性的进一步研究。

Further studies on the properties of glucose 6-phosphate dehydrogenase from the coccidium Eimeria stiedai (Protozoa).

作者信息

Frandsen J C

机构信息

USDA-ARS-SR, Regional Parasite Research Laboratory, Auburn, AL 36830.

出版信息

Comp Biochem Physiol B. 1978;60(3):303-7. doi: 10.1016/0305-0491(78)90105-0.

Abstract
  1. Glucose 6-phosphate dehydrogenase from Eimeria stiedai does not reduce NAD or any of its analogs tested. It does reduce NADP and its thionicotinamide and 3-acetylpyridine analogs. 2. It will accept D-glucose as substrate, but not 2-deoxy-D-glucose, glucose 1-phosphate, or 2-deoxy-D-glucose 6-phosphate. 3. Its response to a number of compounds that activate or inhibit the enzyme from other organisms has been determined. 4. The molecular weight is ca. 240,000 by gel chromatography, and only one isoenzyme could be detected by disc electrophoresis. 5. The enzyme resists conditions that commonly cause dissociation to lighter weight active forms.
摘要
  1. 来自斯氏艾美耳球虫的葡萄糖6-磷酸脱氢酶不还原NAD或所测试的任何其类似物。它确实能还原NADP及其硫代烟酰胺和3-乙酰吡啶类似物。2. 它可将D-葡萄糖作为底物,但不能利用2-脱氧-D-葡萄糖、葡萄糖1-磷酸或2-脱氧-D-葡萄糖6-磷酸。3. 已确定了它对许多激活或抑制其他生物体中该酶的化合物的反应。4. 通过凝胶色谱法测定其分子量约为240,000,并且通过圆盘电泳仅能检测到一种同工酶。5. 该酶能抵抗通常会导致解离为较轻分子量活性形式的条件。

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