Partial characterization of the carbohydrate units of rat intestinal sucrase--isomaltase.
Sucrase--isomaltase was purified from rat intestinal microvillus membranes after injection of D-[2-3H]mannose and L-[6-3H]fucose, using a column of monoclonal antibody-protein A-Sepharose. After Pronase digestion and gel filtration of the glycopeptides labelled from both precursors, a major part of the radioactivity was recovered in asparagine-linked complex oligosaccharides, and a smaller amount in partially alkali-labile high-molecular-weight glycopeptides. Only a small amount of [3H]mannose was found in endo-beta-N-acetylglucosaminidase H-sensitive high-mannose oligosaccharides.
D000818:Animals; D002241:Carbohydrates / Q000032:analysis*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005643:Fucose / Q000378:metabolism; D007413:Intestinal Mucosa / Q000201:enzymology*; D008358:Mannose / Q000378:metabolism; D008871:Microvilli / Q000201:enzymology; D009097:Multienzyme Complexes / Q000302:isolation & purification; D051381:Rats; D011919:Rats, Inbred Strains; D013394:Sucrase-Isomaltase Complex / Q000302:isolation & purification
D002241:Carbohydrates; D009097:Multienzyme Complexes; D005643:Fucose; D013394:Sucrase-Isomaltase Complex; D008358:Mannose