Journal article
Structural studies on the O-glycosidically linked carbohydrate chains of glucoamylase G1 from Aspergillus niger
Glucoamylase G1 from Aspergillus niger contains an unusual type of carbohydrate-protein linkage, involving mannose O-glycosidically linked to serine and threonine. The majority of the neutral oligosaccharides of glucoamylase G1 are located in a region of about 70 amino acid residues which carries about 35 oligosaccharide units [(1983) Carlsberg Res.
Commun. 48, 517-527]. Structural analysis was performed on the O-linked carbohydrates of a tryptic fragment from glucoamylase G1 comprising the segment characterized by a high degree of glycosylation. The carbohydrate structures released by trifluoroacetolysis were elucidated using sugar analysis, methylation analysis, mass spectrometry, chromium trioxide oxidation, digestion with alpha-mannosidase and 1H-NMR spectroscopy.
The following structures could be identified. (formula; see text)
Language: | English |
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Year: | 1984 |
Pages: | 463-467 |
ISSN: | 14321033 and 00142956 |
Types: | Journal article |
DOI: | 10.1111/j.1432-1033.1984.tb08578.x |
Aspergillus niger Carbohydrates Chemical Phenomena Chemistry Chromium Chromium Compounds Glucan 1,4-alpha-Glucosidase Glucosidases Glycosides Magnetic Resonance Spectroscopy Mannosidases Mass Spectrometry Methylation Oxidation-Reduction Trifluoroacetic Acid alpha-Mannosidase chromium trioxide