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Determination of covalently bound myo ‐inositol in bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase
Author(s) -
Taguchi Ryo,
Kawase Mamoru,
Ikezawa Hiroh
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81173-0
Subject(s) - chemistry , inositol , covalent bond , alkaline phosphatase , biochemistry , acetylcholinesterase , deamination , enzyme , receptor , organic chemistry
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.