Affinity chromatography of Lactobacillus Phosphofructokinase on Blue Dextran-Sepharose
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概要
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Phosphofructokinase (EC 2.7.1.11) of several homolactic acid bacteria was adsorbed on blue dextran-Sepharose. All the enzymes adsorbed were quantitatively eluted with 10 mM Tris-HCl buffer (pH 7.5) containing 1 M KCl. At a concentration of 1 mM, ATP and fructose 6-phosphate eluted the enzyme of Lactobacillus plantarum AHU 1047,but ADP, AMP, guanine nucleotides, pyridine nucleotides and fructose 1,6-bisphosphate did not. The enzymes of the other strains of L. plantarum were also eluted with 1 mM ATP in good yields. By single step purification using elution with a linear gradient of 0 and 1 M KCl, phosphofructokinase of L. plantarum AHU 1047 was purified approximately 554-fold with about 60% yield. The resulting enzyme appeared to be homogeneous on 7% polyacrylamide gel disc electrophoresis at pH 9.4.
- 公益社団法人日本生物工学会の論文
- 1977-12-25
著者
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Eguchi Yoshitomo
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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Eguchi Yoshitomo
Department Of Microbial Engineering And Technology Faculty Of Agriculture Hokkaido University
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Kawai Keiichi
Department Of Bioresources Utilization Faculty Of Agriculture Gifu University
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Kawai Keiichi
Department Of Microbial Engineering And Technology Faculty Of Agriculture Hokkaido University
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