Determination of covalently bound myo‐inositol in bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase

FEBS Letters

Taguchi, Ryo¹  Ikezawa, Hiroh¹  Kawase, Mamoru¹ 

[1] Faculty of Pharmaceutical Sciences, Nagoya City University, Mizuho-ku, Nagoya 467, Japan

关键词: Alkaline phosphatase;    Acetylcholinesterase;    Phosphatidylinositol-specific phospholipase C;    Phosphatidylinositol anchor;   

DOI  :  10.1016/0014-5793(87)81173-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase were purified to a homogeneous state. By using gas chromatography-mass spectrometry, we demonstrated the presence of covalently bound myo-inositol in these purified enzymes. The quantitative data suggest that one molecule of myo-inositol is bound to each subunit of these enzyme proteins. The covalently bound inositol was removed from these enzyme molecules by deamination with nitrous acid, suggesting the possibility that myo-inositol is directly bound to amino sugar.

【 授权许可】

Unknown