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. 1981 Mar;78(3):1557–1561. doi: 10.1073/pnas.78.3.1557

Immunological evidence for the transmembrane nature of the rat liver receptor for asialoglycoproteins.

J Harford, G G Ashwell
PMCID: PMC319170  PMID: 6262814

Abstract

Antibodies raised in goats against the rat hepatic receptor for desialylated glycoproteins were perfused through a rat liver and were specifically retained by the liver. These antireceptor antibodies also bound specifically to hepatocyte plasma membranes oriented with their cytoplasmic surface outward on polylysine-derivatized beads. These two phenomena were judged to be properties of distinct subpopulations of the antibody preparation because: (i) maximal adsorption of antibodies with membranes on polylysine beads did not affect subsequent retention by the perfused liver, and (ii) whereas perfusion resulted in a depletion of antibodies capable of blocking ligand binding, adsorption by the everted membrane preparation led to a relative enrichment of blocking antibodies. These results are interpreted as indicative of distinct antigenic determinants of the receptor being present on the two faces of the membrane and demonstrate a transbilayer disposition of the asialoglycoprotein receptor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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