Some Further Properties of the Partially Purified γ-Aminobutyrate Transaminase from Bacillus cereus Strain K-22
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概要
- 論文の詳細を見る
GABA transaminase was purified about 70-fold over a crude extract of Bacillus cereus K-22 and the stoichiometries of the forward and reverse enzyme reactions were established. This enzyme required pyridoxal-5'-phosphate as a cofactor and the molecular weight of this enzyme was estimated to be 130,000 by gel filtration. This enzyme was inhibited by sulfhydryl inhibitor and the inhibition was restored by sulfhydryl compounds. The enzyme was more active and exhibited higher stability against heat treatment in the presence of sulfhydryl compounds.
- 大阪府立大学の論文
- 1977-03-31
著者
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Nakano Yoshihisa
Nutrition Laboratory College Of Agriculture
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Tokunaga Masao
Nutrition Laboratory College Of Agriculture:(present Address)department Of Parasitology Tokai Univer
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Tokunaga Hiroko
Nutrition Laboratory College Of Agricurture:(present Address)department Of Biology Faculty Of Scienc
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KITAOKA Shozaburo
Nutrition Laboratory, College of Agricurture
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Kitaoka Shozaburo
Nutrition Laboratory College Of Agriculture
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