The anguish of the veterans.
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Biomedical subjects
Publications and source records attributed to F Downs.
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A secretory glycoprotein was isolated from the hamster sublingual gland. It contains 65% carbohydrates, the remainder being protein. The principal type of sialic acid was identified as N-acetylneuraminic acid with about 1/4 of the molecules O-acetylated. The hexosamine occurs mainly as N-acetylgalactosamine; other sugars present are galactose and fucose. The carbohydrate side chains are linked to the protein core by an O-glycosyl linkage between seryl and threonyl residues and N-acetylgalactosamine. The glycoprotein has an apparent molecular weight of 330,000. The sialogly coprotein may act as a biological antifreeze. Relevant differences in the chemical composition of the secretory glycoproteins of the sublingual and submaxillary salivary glands of this species are briefly discussed.
The carbohydrate side chains of mucus-type glycoproteins are O-glycosidic bonds between N-acetylgalactosamine to the hydroxyl groups of serine and threonine in the protein core. The alkaline catalyzed beta-elimination reaction, in the presence of sodium borohydride, is used for determining the number of side chains. The present paper presents a study of the quantitativeness of the alkaline borohydride procedure, using four parameters: the loss of seryl and threonyl residues, the formation of alanine and 2-aminobutanoic acid; the decrease in N-acetylhexosamine and the recovery of the amino sugar alcohols. Bovine, ovine and porcine submandibular glycoproteins were studied. Evidence is presented for the existence of N-acetylglucosamine involvement in O-glycosidic linkages to serine and threonine. Results for the relative rates of beta-elimination indicate that serine-linked glycosides are released more rapidly than threonine-linked glycosides.
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