STRUCTURES OF NEUTRAL O-LINKED POLYLACTOSAMINOGLYCANS ON HUMAN SKIM MILK MUCINS - A NOVEL TYPE OF LINEARLY EXTENDED POLY-N-ACETYLLACTOSAMINE BACKBONES WITH GAL-BETA-(1-4)GLCNAC-BETA-(1-6) REPEATING UNITS

  • 15 January 1989
    • journal article
    • research article
    • Vol. 264  (2) , 872-883
Abstract
O-Linked oligosaccharides were isolated from human skim milk mucins and from mucin-derived glycopeptides by reductive .beta.-elimination. The released alditols were fractionated by DEAE-Sephadex chromatography and purified by high performance liquid chromatography on primary amine bonded phase. The structures of the major neutral oligosaccharide alditols could be established by fast atom bombardment and electron impact mass spectrometry, combined with methylation analysis, 500-MHz 1H nuclear magnetic resonance spectroscopy, and endo-.beta.-galactosidase (from Bacteroides fragilis, EC 3.2.1.103) digestion. Major O-glycosidically linked oligosaccharides on skim milk mucins are of the Gal.beta.(1-3)[GlcNAc.beta.(1-6)] GalNAc core type 2 and exhibit linearly extended backbone chains of the poly N-acetyllactosamine type comprising up to at least four repeating units, which are linked by the hitherto unknown sequence GlcNAc.beta.(1-6)Gal rather than GlcNAc.beta.(1-3)Gal. A considerable portion of neutral alditols is represented by branched isomers of the linear species, which are distinguished by their content of 3,6-disubstituted galactose and their partial resistance to endo-.beta.-galactosidase digestion.

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