O-Glycosidic linkages

Based on the nature of the linkage between their polypeptide chains and their oligosaccharide chains, glycoproteins can be divided into three major classes (Figure 47-1) (1) those containing an O-glycosidic linkage (ie,... 

GLYCOPROTEINS CONTAIN SEVERAL TYPES OF O-GLYCOSIDIC LINKAGES... 

Similarly, ketose sugars participate in polysaccharide formation by reaction of their ano-meric carbon with a hydroxyl of another monosaccharide to create a ketal linkage. The acetal and ketal bonds within polysaccharides are termed o-glycosidic linkages. 

Polysaccharide solubility in aqueous solutions usually is dependent on polymer size and its allied three-dimensional structure. Even water-insoluble carbohydrates may be solubilized by controlled hydrolysis of o-glycosidic linkages to create smaller polysaccharide molecules. Thus, cellulose may be solubilized by heating in an alkaline solution until the polymers are broken up sufficiently to reduce their average molecular weight. Many such soluble forms of common polysaccharides are available commercially. 

III. 3-6>-Glycopeptides of l-Serine or l-Threonine 1. Formation of the 3-O-Glycosidic Linkage... 

For glycoproteins, the formation of anhydro rings from hexosamine residues is important in chromogen formation, especially in relation to the Ehrlich reaction and its modifications (3). / -Elimination is involved in the removal of oligosaccharide or polysaccharide chains from the protein core of glycoproteins when they are attached by O-glycosidic linkages to serine or threonine residues. A subsequent -elimination may also... 

On the basis of the close correlation between the number of hydroxy-amino acids in bovine submaxillary mucin and the number of hexosamine and sialic acid residues, Hashimoto and Pigman (34) proposed that an O-glycosidic linkage was the only one that could be present in large amounts. Anderson et al. (38) reported a disappearance of much of the serine after incubation of the proteoglycan of chondroitin sulfate with alkali and suggested that this loss resulted from a -elimination reaction. 

Direct proof for the existence of O-glycosidic linkages involving the hydroxyl groups of serine and threonine was provided simultaneously from three laboratories. Anderson et al. (39) reported partial losses of serine and threonine after treatment with 0.52V NaOH (or 0.452V KOH) at 4°C or room temperature for about 20 hours. Subsequent reduction with platinum showed formation of some alanine and < -aminobutyric acid. Harbon et al (40) treated ovine submaxillary glycoprotein at pH 12.8 for 45 minutes at 70 °C. The serine and threonine content decreased by 78 and 60%, respectively. Treatment of this product with 0.1M sulfite, (pH 9, 24 hours, room temperature) caused a conversion of the dehydroserine residues to cysteic acid, but had no action on the dehydrothreonine residues. This reaction has been further studied by Simpson et al. (41). 

Glycoproteins in the secretory pathway receive GalNac in O-glycosidic linkage from UDP-GalNAc via a transferase that acts directly on certain Ser or Thr residues of proteins. 

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