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Turnover studies of human intestinal brush border membrane glycoproteins in organ culture

Kedinger, M. and Hauri, H. P. and Haffen, K. and Green, J. R. and Grenier, J. F. and Hadorn, B.. (1979) Turnover studies of human intestinal brush border membrane glycoproteins in organ culture. Enzyme, Vol. 24, H. 2. S. 96-106.

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Official URL: http://edoc.unibas.ch/dok/A5257850

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Abstract

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 double isotope 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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Pharmacology/Neurobiology (Hauri)
UniBasel Contributors:Hauri, Hans-Peter
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:Karger
ISSN:0013-9432
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:22
Deposited On:22 Mar 2012 13:29

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