Some Properties of Pantothenate Synthetase Partially Purified from Escherichia coli B
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概要
- 論文の詳細を見る
Pantothenate synthetase was purified 285-fold from E. coli B (IFO 13168) but the preparation was not yet homogeneous containing minute amounts of other proteins. The enzyme was most active at pH 10.0 and at 30℃. Revised Km values of this enzyme toward substrates and co-factors are given. The enzyme was inhibited by most metal cations studied and by metal-chelating agents but not by thiol reagents. Substrate analogs and reaction products were also inhibiting on the enzyme.
- 大阪府立大学の論文
- 1975-03-31
著者
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Miyatake K
Osaka Prefecture Univ. Osaka Jpn
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NAKANO Yoshihisa
Graduate School of Life and Environmental Sciences of Osaka Prefecture University
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Nakano Yoshihisa
Nutrition Laboratory College Of Agriculture
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Miyatake Kazutaka
Nutrition Laboratory College Of Agriculture
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Kitaoka S
Univ. Osaka Prefecture Osaka Jpn
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Kitaoka Shozaburo
Nutrition Laboratory College Of Agriculture
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