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- W1969138847 abstract "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." @default.
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- W1969138847 date "1987-12-10" @default.
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- W1969138847 title "Determination of covalently boundmyo-inositol in bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase" @default.
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- W1969138847 doi "https://doi.org/10.1016/0014-5793(87)81173-0" @default.
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