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.
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Research Article| August 01 1981
Partial characterization of the carbohydrate units of rat intestinal sucrase-isomaltase
Biochem J (1981) 197 (2): 511–514.
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A Herscovics, A Quaroni, B Bugge, K Kirsch; Partial characterization of the carbohydrate units of rat intestinal sucrase-isomaltase. Biochem J 1 August 1981; 197 (2): 511–514. doi: https://doi.org/10.1042/bj1970511
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