Purification and Characterization of 6-Phosphogluconate Dehydrogenase from Phormidium sp.
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概要
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A procedure for the purification of 6-phosphogluconate dehydrogenase from the cyanobacterium Phormidium sp. is described. The molecular weight of the native enzyme was 104, 000 by gel filtration, and SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of two subunits with an identical molecular weight of 52, 000. The optimum pH of the reaction was 8.0. The Km values for 6-phosphogluconate and NADP were 3.6×10-5M and 1.3×10-5M, respectively. The enzyme showed no Mg2+ requirement for the activity, but was activated by Mn2+ and Ca2+. The enzyme was inhibited by sulfhydryl reagents, indicating that a sulfhydryl group may be involved in the active site of the enzyme. The enzyme was also inhibited by NADPH2, ATP, and the intermediates formed during photosynthesis. The substrate 6-phosphogluconate and cofactor NADP partially protected the enzyme from inactivation. The enzyme had enzymological and physicochemical properties similar to enzymes isolated from other sources.
- 社団法人 日本農芸化学会の論文
著者
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Sawa Yoshihiro
Laboratory of Applied Biological Science, Faculty of Agriculture
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Ochiai Hideo
Laboratory Of Applied Biological Science Faculty Of Agriculture Shimane University
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OCHIAI Hideo
Laboratory of Biochemistry, College oj Agriculture, Shimane University
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SUZUKI Kanji
Laboratory of Biochemistry, College oj Agriculture, Shimane University
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SAWA Yoshihiro
Laboratory of Biochemistry, College oj Agriculture, Shimane University
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