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Struktur der Zellwandpolysaccharide in der Futtereiweiß‐Hefe Candida spec. H. III. Charakterisierung unterschiedlicher Phosphatbindungen im Mannan‐Protein‐Phosphat‐Komplex
Author(s) -
Grimmecke H. D.,
Meyer H.,
Scheller D.,
Reuter G.
Publication year - 1981
Publication title -
zeitschrift für allgemeine mikrobiologie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0044-2208
DOI - 10.1002/jobm.19810210305
Subject(s) - chemistry , phosphodiester bond , mannan , threonine , polyphosphate , hydrolysis , biochemistry , mannose , pronase , nuclear magnetic resonance spectroscopy , serine , phosphate , stereochemistry , polysaccharide , phosphorylation , enzyme , trypsin , rna , gene
The 31 P‐NMR spectra of the proteophosphomannan (PPM) and also that of mildly hydrolyzed PPM demonstrated phosphomonoester (in both preparations), acid labile and acid stable phosphodiester linkage, and polyphosphate. Decreasing in size by pronase digestion, separation, purification and characterization of the high and low molecular phosphates by 31 P‐NMR spectroscopy and chemical analysis revealed the mannan protein is phosphorylated in the N‐glycosidically linked carbohydrate parts and in the O‐glycosidically linked oligosaccharides. Another phosphate serves as a bridge between the serine of the protein and mannose, mannobioses and mannotrioses and between the threonine and a lipophilic acylglycerid unit. The origin of the polyphosphates has been discussed.