Affinity Chromatography of Glyceraldehyde 3-Phosphate Dehydrogenase on Blue Dextran-Sepharose
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概要
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Glyceraldehyde 3-phosphate dehydrogenases (EC 1.2.1.12) of several lactic acid bacteria were adsorbed on Blue Dextran-Sepharose 4B. The adsorbed enzymes were completely eluted from the Blue Dextran-Sepharose column with 1 M KCl in 10 mM Tris-HCl buffer (pH 7.5). Glyceraldehyde 3-phosphate dehydrogenase of Lactobacillus plantarum AHU 1047 was selectively eluted with low concentration (1 mM) of NAD, NADH, NADP, NADPH or ATP in the buffer. The recoveries of enzyme were practically quantitative (>80%). A two-step procedure using ammonium sulfate fractionation and 0 to 1 mM NADH gradient elution from Blue Dextran-Sepharose column yielded a 46.5-fold purification of glyceraldehyde 3-phosphate dehydrogenase with 62.6% recovery. Cibacron Blue F3GA, the chromophore of Blue Dextran, inhibited the enzyme competitively with respect to NAD.
- 公益社団法人日本生物工学会の論文
- 1980-12-25
著者
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Eguchi Yoshitomo
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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Saito Yoshitaka
Show Brand Milk Products Co. Ltd.
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Kawai Keiichi
(present Address)department Of Agricultural Chemistry Faculty Of Agriculture Gifu University
関連論文
- Affinity of Leuconostoc Phosphoglycerate Mutase for Blue Dextran-Sepharose
- Interaction of Lactobacillus plantarum Phosphoglycerate Kinase with Cibacron Blue F3GA
- Affinity chromatography of Lactobacillus Phosphofructokinase on Blue Dextran-Sepharose
- Affinity Chromatography of Lactobacillus Phosphoglycerate Kinase on Blue Dextran-Sepharose
- Affinity Chromatography of Glyceraldehyde 3-Phosphate Dehydrogenase on Blue Dextran-Sepharose
- Specific Elution of Bacillus Phosphofructokinase from Blue Dextran-Sepharose by the Formation of a Dead-end Complex
- Cold Resistant Mutants of Escherichia colic
- Genetic Mapping of Cold Resistance Gene of Escherichia coli
- Interaction of Phosphoglycerate Kinase from Escherichia coli with Cibacron Blue