Thiol-Dependent Subunit Interactions of a Major Fat Cell Plasma Membrane Glycoprotein

References

• Carter J. R., Martin O. B. The effect of sulfhydryl blockade on insulin action and glucose transport in isolated adipose tissue cells. Biochim. Biophys. Acta 1969; 177: 521–526
   Google Scholar
• Cuatrecasas P. Interaction of concanavalin A and wheat germ agglutinin with the insulin receptor of fat cells and liver. J. Biol. Chem. 1973; 248: 3528–3534
   PubMed Web of Science ®Google Scholar
• Czech M. P. Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system. J. Biol. Chem. 1976; 251: 1164–1170
   PubMed Web of Science ®Google Scholar
• Czech M. P., Lynn W. S. The plasma membrane of isolated fat cells. J. Biol. Chem. 1973; 248: 5081–5088
   Google Scholar
• Czech M. P., Lynn W. S. Studies on the topography of the cell plasma membrane. Biochemistry 1973; 12: 3597–3601
   Google Scholar
• Czech M. P., Lynn W. S. Stimulation of glucose metabolism by lectins in isolated white fat cells. Biochim. Biophys. Acta 1973; 297: 368–377
   Google Scholar
• Czech M. P., Lynn W. S. Biology and Chemistry of Eucaryotic Cell Surfaces, E. Y.C. Lee, E. E. Smith. Academic Press, New York 1974; 360
   Google Scholar
• Czech M. P., Lawrence J. C., Jr., Lynn W. S. Activation of hexose transport by concanavalin A in isolated brown fat cells. J. Biol. Chem. 1974; 249: 7499–7505
   Google Scholar
• Czech M. P., Lawrence J. C., Lynn W. S. Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin. Proc. Natl. Acad. Sci. USA 1974; 71: 4173–4177
   PubMed Web of Science ®Google Scholar
• Furthmayr H., Marchesi V. T. Subunit Structure of Human Erythrocyte Glycophorin A. Biochemistry 1976; 15: 1137–1143
   PubMed Web of Science ®Google Scholar
• George J. M. Effect of Mercury on Response of Isolated Fat Cells to Insulin and Lipolytic Hormones. Endocrinology 1971; 89: 1489–1498
   Google Scholar
• Greenbaum C. J., Shanahan M. F., Pillion D. J., Czech M. P. Selective Extraction of an Intrinsic Fat-Cell Plasma-Membrane Glycoprotein by Triton X-100. FEBS Lett. 1978; 83(1)71–75
   Google Scholar
• Hawksley C. A., Guggenheim N. Z., Czech M. P. 1978, Unpublished data
   Google Scholar
• Hynes R. O., Destree A. Extensive disulfide bonding at the mammalian self surface. Proc. Natl. Acad. Sci. USA 1977; 74: 2855–2859
   PubMed Web of Science ®Google Scholar
• Jackson R. L., Segrest J. P., Kahane I., Marchesi V. T. Studies on the major sialoglycoprotein of the human red cell membrane. Isolation and characterization of tryptic glycopeptides. Biochemistry 1973; 12: 3131–706
   Google Scholar
• Katzen H. M., Soderman D. D. Interaction of carbohydrate binding sites on concanavalin A-agarose with receptors on adipocytes studied by buoyant density method. Biochemistyr 1975; 14: 2293–2298
   Google Scholar
• Keski-Oja J., Mosher D. F., Vaheri A. Dimeric character of fibronectin, a major cell surface-associated glycoprotein. Biochem. Biophys. Res. Commun. 1977; 74: 699–706
   PubMedGoogle Scholar
• Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Marton L. S. G., Garvin J. E. Subunit structure of the major human erythrocyte glycoprotein: depolymerization by heating ghosts with sodium dodecyl sulfate. Biochem. Biophys. Res. Commun. 1973; 52: 1457–1462
   PubMedGoogle Scholar
• Marchesi V. T., Andrews E. P. Glycorproteins: isolation from cell membranes with lithium diiodosalycylate. Science 1971; 174: 1247–1248
   PubMed Web of Science ®Google Scholar
• Minemura T., Crofford O. B. Insulin-receptor interaction in isolated fat cells. J. Biol. Chem. 1969; 244: 5181–5188
   Google Scholar
• Phillips D. R., Agin P. P. Platelet plasma membrane glyco-proteins. J. Biol. Chem. 1977; 252: 2121–2126
   PubMed Web of Science ®Google Scholar
• Presant C. A., Parker S. Surface alterations in calf lymphocytes oxidized by sodium periodate. J. Biol. Chem. 1975; 251: 1864–1870
   Google Scholar
• Rodbell M. Metabolism of isolated fat cells. J. Biol. Chem. 1964; 239: 375–380
   PubMed Web of Science ®Google Scholar
• Shanahan M. F., Czech M. P. Purification and reconstitution of the adipocyte plasma membrane D-glucose transport system. J. Biol. Chem. 1978; 252: 8341–8343
   Google Scholar
• Silverberg M., Furthmayr H., Marchesi V. T. The effect of carboxymethylating a single methionine residue on the subunit interactions of glycophorin A. Biochemistry 1976; 15: 1448–1454
   Google Scholar
• Steck T. L., Yu J. Selective solubilization of proteins from red blood cell membranes by protein perturbants. J. Supramol. Struct. 1973; 1: 220–232
   PubMedGoogle Scholar
• Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc. Natl. Acad. Sci. USA 1975; 72: 2964–2968
   PubMed Web of Science ®Google Scholar
• Trosper T., Levy D. Characterization of the surface protein components in adipocyte plasma membranes. Biochemistry 1974; 13: 4284–4290
   Google Scholar
• Tuech J. K., Morrison M. Human erythrocyte membrane sialoglycoproteins: a study of interconversion. Biochem. Biophys. Res. Commun. 1974; 59: 352–360
   Google Scholar
• Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 1969; 244: 4406–4412
   PubMed Web of Science ®Google Scholar
• Yu J., Steck T. L. Isolation and characterization of band 3, the predominant polypeptide of the human erythrocyte membrane. J. Biol. Chem. 1975; 250: 9170–9175
   Google Scholar
• Yu J., Steck T. L. Associations of band 3, the predominant polypeptide of the human hrythrocyte membrane. J. Biol. Chem. 1975; 250: 9176–9185
   Web of Science ®Google Scholar
• Zacharius R. M., Zell T. E., Morrison J. H., Woodlock J. J. Glycoprotein staining following electrophoresis on acrylamide gels. Anal. Biochem. 1969; 30: 148–152
   PubMed Web of Science ®Google Scholar