[Structure of the cell wall polysaccharide in the food protein yeast Candida spec H. III. Characterization of different phosphate bonds in the mannan-protein-phosphate complex].
The 31P-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 31P-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.
D002175:Candida / Q000032:analysis*; D002473:Cell Wall / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D005656:Fungal Proteins / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D008562:Membrane Glycoproteins; D010710:Phosphates / Q000032:analysis*; D011509:Proteoglycans / Q000032:analysis*
D005656:Fungal Proteins; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D010710:Phosphates; D011509:Proteoglycans; C025363:mannoproteins
Struktur der Zellwandpolysaccharide in der Futtereiweiss-Hefe Candida spec. H. III. Charakterisierung unterschiedlicher Phosphatbindungen im Mannan-Protein-Phosphat-Komplex.