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ファイル
言語
英語
著者
佐伯 孝雄
片桐 義博
林原 正和
沢田 英夫
原 明
臼井 茂之
内容記述(抄録等)
The solubilization, purification and property of hexose 6-phosphate dehydrogenase from guinea pig liver microsomes is described. The enzyme was effectively solubilized by ammonium hydroxide in the presence of 0.5% detergent, and highly purified. The enzyme showed a different pH dependency for various substrates. The optimum pH for galactose 6-phosphate, glucose 6-phosphate and glucose was 8.5,10.2 and more alkaline, respectively. Km values for the substrates were also changed, pH dependently. The enzyme exhibited the lowest Km values in an order of 10^<-6>M for glucose 6-phosphate at pH 7.0. The enzyme activity was inhibited by CaCl_2 and HgCl_2,but other metal compounds, steroids, pCMB and NADPH did not inhibit the activity. The antibody against the purified enzyme inhibited the enzyme activity of Triton X-100 treated microsomes while the inhibition of the enzyme activity of intact microsomes by antibody was very low.
主題
H6PD
guinea pig liver
solubilization and properties
掲載誌名
Shimane journal of medical science
6
1
開始ページ
1
終了ページ
12
ISSN
03865959
ISSN(Online)
24332410
発行日
1982-06-01
NCID
AA00841586
出版者別表記
Shimane Medical University
資料タイプ
紀要論文
ファイル形式
PDF
著者版/出版社版
出版社版
部局
医学部
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