Abstract
Glycoprotein synthesis was measured by the incorporation of 14-C-glucosamine into total acid precipitable protein of jejunal explants cultured in vitro. The rate of glucosamine incorporation remained constant up to 48 hours. During this time a continuous release of glycoprotein into the culture medium was observed. Pulse-chase experiments indicated that the mean half life of overall labelled tissue glycoprotein was about 20 hours. SDS-polyacrylamide-gel-electrophoresis of the isolated brush border membrane showed that all major protein bands of high molecular weight had incorporated 14-C-glucosamine. These proteins were identified as maltase-glucoamylase, lactase, sucrase-isomaltase, enterokinase and alkaline phosphatase. Specific enzyme activity could not be assigned to the two remaining labelled bands. After 5 hours of culture lactase showed the highest glucosamin incorporation. These results indicate that the organ culture method is suitable for studying the biosynthesis, of human intestinal brush border enzymes in biopsies from patients with intestinal malabsorption syndromes.
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Hauri, H., Kedinger, M., Haffen, K. et al. 49: Glycoprotein synthesis by human small intestine in organ culture. Pediatr Res 10, 879 (1976). https://doi.org/10.1203/00006450-197610000-00047
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DOI: https://doi.org/10.1203/00006450-197610000-00047
