Turnover in organ culture of human small intestinal membrane glycoproteins was measured by the pulse-chase technique, using 14C-glucosamine, 14C-fucose or 14C-leucine as tracers. Apparently, low degradation rates were found for the major high-molecular-weight proteins which co-migrated on SDS-polyacrylamide gels with maltase-glucoamylase, lactase-phlorizin-hydrolase and sucrase-isomaltase enzymic activities. In contrast, an unidentified glycoprotein appearing on gels next to alkaline phosphatase exhibited a higher degradation rate with an apparent half-life of about 30 h, this being similar to the half-life of total glycoprotein as measured in mucosal homogenates. The results obtained with the pulse-chase technique were confirmed by doubleisotope experiments using 14C-leucine and 3H-leucine as tracers. These findings indicate that in organ culture there is a low basic turnover of human intestinal membrane glycoproteins which co-migrate on gels with known glycosidase enzymic activities.

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