Open AccessReconstitution of the hepatic asialoglycoprotein receptor with phospholipid vesicles.
Author(s) -
Richard D. Klausner,
Kenneth R. Bridges,
Hajime Tsunoo,
Robert Blumenthal,
John N. Weinstein,
Gilbert Ashwell
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.9.5087
Subject(s) - asialoglycoprotein receptor , vesicle , phospholipid , circular dichroism , biophysics , chemistry , biochemistry , protein–lipid interaction , conformational change , lipid bilayer , membrane protein , integral membrane protein , biology , membrane , in vitro , hepatocyte
A solubilized detergent-free preparation of the hepatic binding protein specific for asialoglycoproteins associates spontaneously with small unilamellar lipid vesicles. This process is independent of the phase transition of the lipid and effectively restores the specific binding activity of the receptor protein. The insensitivity of the resulting lipid-protein complex to ionic strength provides evidence for a hydrophobic interaction. There is a perturbation of the lipid phase transition concomitant with addition of the protein. Circular dichroism studies indicate that the protein undergoes a conformational change on association with lipid. Binding of specific ligand produces further physical changes in the receptor as indicated by alterations in the tryptophan fluorescence quenching pattern.