Determination of covalently bound myo-inositol in bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase.
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.
Taguchi
R
R
Faculty of Pharmaceutical Sciences, Nagoya City University, Japan.
Kawase
M
M
Ikezawa
H
H
D000110:Acetylcholinesterase / Q000032:analysis*; D000469:Alkaline Phosphatase / Q000032:analysis*; D000818:Animals; D002417:Cattle; D003641:Deamination; D004912:Erythrocytes / Q000201:enzymology*; D008401:Gas Chromatography-Mass Spectrometry; D007294:Inositol / Q000032:analysis* / Q000378:metabolism; D007668:Kidney / Q000201:enzymology*; D009608:Nitrous Acid; D013552:Swine
D007294:Inositol; D000110:Acetylcholinesterase; D000469:Alkaline Phosphatase; D009608:Nitrous Acid