玉米胞质6-磷酸葡萄糖酸脱氢酶同工酶的纯化与特性分析
Purification and characterization of cytosolic 6-phosphogluconate dehydrogenase isozymes from maize.
作者信息
Bailey-Serres J, Nguyen M T
机构信息
Department of Botany and Plant Sciences, University of California, Riverside, California 92521.
出版信息
Plant Physiol. 1992 Nov;100(3):1580-3. doi: 10.1104/pp.100.3.1580.
Abstract
Cytosolic isozymes of 6-phosphogluconate dehydrogenase were purified from roots of maize (Zea mays L.). The final preparation contained two 55-kD proteins. Affinity-purified dehydrogenases from a maize line that is null for both cytosolic 6-phosphogluconate dehydrogenase isozymes (Pgd1-null, Pgd2-null) lacked the 55-kD proteins. The substrate kinetics of the purified enzyme were determined.
摘要
从玉米（Zea mays L.）根中纯化出6-磷酸葡萄糖酸脱氢酶的胞质同工酶。最终制剂含有两种55-kD蛋白。从一个对两种胞质6-磷酸葡萄糖酸脱氢酶同工酶均无效的玉米品系（Pgd1无效、Pgd2无效）亲和纯化得到的脱氢酶缺乏55-kD蛋白。测定了纯化酶的底物动力学。
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