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Isolation of a very high molecular weight polylactosamine from an ovarian cyst mucin of blood group

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7108779
Treatment of a blood group A active ovarian cyst mucin glycoprotein with alkaline borohydride under conditions expected to cleave-O-glycosidically linked carbohydrate chains releases a polysaccharide of average molecular weight 25,000 daltons. It contains no peptide or mannose at the 1% level and carbohydrate analysis gives fuc:galNAc:gal:glcNAc in the ratio of 1:1:2.5:2.5. The /sup 13/C and /sup 1/H NMR spectra show that the polysaccharide has non-reducing terminal side chains of the structure galNAc(..cap alpha..-1 ..-->.. 3)(fuc(..cap alpha..-1 ..-->.. 2)) gal(..beta..-1 ..-->.. 3) glcNAc (i.e. a type 1 chain). Periodate oxidation removes all the fucose and galNAc from the non-reducing terminal but leaves intact the backbone composed of ..beta..-linked gal and glcNAc as would be expected for a polylactosamine. They conclude that this is a high molecular weight polylactosamine which is related to the asparagine linked polylactosamine chains of cell surface glycoproteins which have been implicated in cell differentiation. However, the blood group A polysaccharide from the ovarian cyst mucin is unique in several respects. It has a much larger molecular weight than even the erythroglycan of the red cell membrane protein, band 3, and is linked to the protein by an -O-glycosidic bond rather than the -N-asparagine linkage of the previously known polylactosamines which have a trimannosyl core. Its blood group A side chains are on a type one core rather than type 2 which is found on other polylactosamines.
Research Organization:
Illinois Institute of Technology, Chicago
OSTI ID:
7108779
Report Number(s):
CONF-8606151-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
Country of Publication:
United States
Language:
English