Abstract
A preparation of human follicle-stimulating hormone has been subjected to methylation analysis by using the methyl sulphinyl carbanion–dimethyl sulphoxide–methyl iodide method. The hydrolysis products of the methylated glycoprotein were reduced, acetylated, analysed by gas-phase chromatography and mass spectrometry and identified by comparison with standards. Methylation analysis demonstrated that (1) the d-galactose, mannose, fucose and 2-amino-2-deoxyglucose units exist in the pyranose forms, (2) the 2-amino-2-deoxyglucose units are N-acetylated, (3) the fucopyranose units occupy terminal non-reducing positions, (4) the d-galactopyranose units are linked in the 1- and 2-positions, (5) the mannopyranose units exist in three forms, some as terminal non-reducing residues, some as 1,6-linked residues and some as 1,3,4-linked branch points, and (6) the 2-acetamido deoxyglucopyranose units are 1,6-linked. These structural assignments are compared with other data previously obtained for the carbohydrate moieties of follicle-stimulating hormone.
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Selected References
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