[Biosynthesis of pulmonary glycoconjugates. Mechanism of glucosylation of protein and lipid acceptors].

In sheep lung microsomes, we have shown that glucosyl-transferases catalize the transfer of glucose from UDP-glucose into four different acceptors. The glucosylated products obtained are as follows: - a glucosyl-phosphoryl-polyprenol (product A) extractable by chloroform/methanol (2:1 by volume). - a product B extractable by chloroform/methanol/water (10:10:3 by volume). The product B was a mixture of five glycolipids, one of them having a chromatographic behaviour similar to the behaviour of a tetrahexosylceramide (asia-lo-GM1). - a product C insoluble in water and organic solvents which has been demonstrated to be a glycoproteinic compound. The molecular weight of this product C was 160 000 as estimated by gel-filtration. The carbohydrate moiety is composed of small oligosaccharides which are found to be attached by O-glycosidic bond to the protein chain. This linkage is not a collagen-like bond.