VITAMINS
Online ISSN : 2424-080X
Print ISSN : 0006-386X
Studies on Properties of Phosphatase of Lactobacillus fermenti Specific for Thiamine diphosphate and Thiamine monophosphate
Masaomi KONDOTomio ICHIKAWAKazue SANOKeiji SANOYasuo KAKIUCHIChikataro KAWASAKI
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1975 Volume 49 Issue 7 Pages 255-258

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Abstract
Properties of phosphatase having specific activity for thiamine diphosphate and thiamine monophosphate were studied. When compared with p-nitrophenylphosphatase of L.fermenti, this phosphatase activity was inhibited by Mg^<2+> and Na_2MoO_4,while the p-nitrophosphatase was activated by Mg^<2+> and not affected by Na_2MoO_4. This enzyme activity was not affected by other phosphate compounds at all. When L.fermenti cells were cultivated with thiamine, the enzyme activity was decreased with increasing amounts of thiamine added to the medium.
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© 1975 THE VITAMIN SOCIETY OF JAPAN

この記事はクリエイティブ・コモンズ [表示 - 非営利 - 改変禁止 4.0 国際]ライセンスの下に提供されています。
https://creativecommons.org/licenses/by-nc-nd/4.0/deed.ja
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