Isolation and partial characterization of the oligosaccharide moieties of rat preputial beta-glucuronidase.
The oligosaccharide alditols of rat preputial gland beta-glucuronidase have been isolated by reductive alkaline hydrolysis of the enzyme followed by gel filtration. Since the product was about decasaccharide in size, and as beta-glucuronidase contains about 20 sugar residues per subunit, the enzyme must contain two oligosaccharides per subunit. Two major subfractions were obtained. Chemical and enzymatic studies on the initial oligosaccharide alditol fraction and on the separated subfractions indicated the presence of a mannosyl-chitobiosyl core and permitted formulation of the following structures for the two different oligosaccharide alditols: Man3 leads to alpha [(alpha Man, GlcNAc) leads to Man] leads to beta GlcNAc leads to beta GlcNAc-ol Man 3 leads to 4 leads to alpha[Man2 leads to alpha Man] leads to beta GlcNAc leads to beta GLcNAc-ol.
D000818:Animals; D002849:Chromatography, Gas; D002850:Chromatography, Gel; D002987:Clitoris; D003208:Concanavalin A / Q000378:metabolism; D005260:Female; D005966:Glucuronidase / Q000302:isolation & purification* / Q000378:metabolism; D009844:Oligosaccharides / Q000032:analysis*; D051381:Rats; D012627:Sebaceous Glands / Q000201:enzymology*
D009844:Oligosaccharides; D003208:Concanavalin A; D005966:Glucuronidase