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J. Biol. Chem., Vol. 267, Issue 4, 2370-2374, 02, 1992

Identification of the protein responsible for hepatic system N amino acid transport activity

BK Tamarappoo, ME Handlogten, RO Laine, MA Serrano, J Dugan and MS Kilberg
Department of Biochemistry and Molecular Biology, J. Hillis Miller Health Center, University of Florida, Gainesville 32610.

In the liver, glutamine utilization may be limited by the rate of transport across the plasma membrane by the System N carrier. System N- mediated transport activity has been solubilized from rat liver plasma membrane, partially purified, and then reconstituted into proteoliposomes. To identify the System N carrier protein, monoclonal antibodies were generated against the protein fraction enriched for System N activity. Two antibodies , 3E1-2 and 1E7-3, inhibited System N activity in hepatocytes. These antibodies also immunoprecipitated System N activity from a mixture of solubilized proteins and were specific for antigen recognition in that neither immunoprecipitated System A activity. The antibody recognized a single protein of molecular size 100 kDa by immunoblot analysis. Recognition of this protein by the antibody increased in parallel with the enrichment of System N activity in solubilized membrane fractions. These data suggest that a 100-kDa plasma membrane protein mediates System N transport activity in rat hepatocytes.
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