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Original Article

Transmembrane helix-helix interactions and accessibility of H2DIDS on labelled band 3, the erythrocyte anion exchange protein

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Pages 173-182 | Received 07 Jun 1994, Published online: 09 Jul 2009

References

  • Bibi E., Kaback H. R. In vivo expression of the lacY gene in two segments leads to functional lac permease. Proceedings of the National Academy of Sciences, USA 1990; 87: 4325–4329
  • Bradford M. M. A rapid and sensitive method for the quantitatión of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976; 72: 248–254
  • Burr F. A., Burr B. Slab gel system for the resolution of oligopeptides below molecular weight of 10 000. Methods in Enzymology 1983; 96: 239–244
  • Cabantchik Z. I., Greger R. Chemical probes for anion transporters of mammalian membranes. American Journal of Physiology 1992; 31: C803–C827
  • Cabantchik Z. I., Rothstein A. Membrane proteins related to anion permeability of human red blood cells I. Localization of disulfonic stilbene binding sites in proteins involved in permeation. Journal of Membrane Biology 1974; 15: 207–226
  • Casey J. R., Reithmeier R. A. F. Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography: oligomeric stability and origin of heterogeneity. Journal of Biological Chemistry 1991; 266: 15726–15737
  • Davio S. R., Low P. S. Characterization of the calorimetric C transition of the human erythrocyte membrane. Biochemistry 1982; 21: 3585–3593
  • Eidelman O., Yanai P., Engelbert H. C., Lang H. G., Greger R., Cabantchik Z. I. Macromolecular conjugates of transport inhibitors: new tools for probing topography of anion transport proteins. American Journal of Physiology 1991; 260: C1094–C1103
  • Engvall E. Enzyme immunoassay ELISA and EMIT. Methods in Enzymology 1980; 70: 419–439
  • Garcia A. M., Lodish H. F. Lysine 539 of human band 3 is not essential for ion transport or inhibition by stilbene disulfonates. Journal of Biological Chemistry 1989; 264: 19607–19613
  • Gilles-Gonzales M., Engelman D., Khorana H. Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure. Journal of Biological Chemistry 1991; 266: 8545–8550
  • Harboe N., Inglid A. Immunization, isolation of immunoglobulins. Estimation of antibody titre. A Manual of Quantitative Immunoelectrophoresis, N. H. Axelson, J. Krall, B. Weeks. Universitetforlaget, Oslo-Bergen-Tromse 1973; 161–164
  • Hennessey J. P., Scarborough G. A. An optimized procedure for sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of hydrophobic peptides from an integral membrane protein. Analytical Biochemistry 1989; 176: 284–289
  • Huang K.-S., Bayley H., Liao M.-J., London E., Khorana H. G. Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. Journal of Biological Chemistry 1981; 256: 3802–3809
  • Jennings M. L., Passow H. Anion transport across the erythrocyte membrane in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4′-diisothiocyano dihydrostilbene-2,2′-disulfonate. Biochimica et Biophysics Acta 1979; 554: 498–519
  • Jennings M. L., Adams-Lackey M., Denney G. H. Peptides of human erythrocyte band 3 protein produced by extracellular papain cleavage. Journal of Biological Chemistry 1984; 259: 4652–4660
  • Jentsch T. J., Garcia A. M., Lodish H. F. Primary structure of a novel 4-acetamido-4′-isothiocyanostilbene-2,2′-disulfonic acid (SITS)-binding membrane protein highly expressed in Torpedo californica electroplax. Biochemical Journal 1989; 261: 155–166
  • Kahn T. W., Engelman D. M. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and complementary five-helix fragment. Biochemistry 1992; 31: 6144–6151
  • Kang D., Okubo K., Hamasaki N., Kuroda N., Shiraki H. A structural study of the membrane domain of band 3 by tryptic digestion. Journal of Biological Chemistry 1992; 267: 19211–19217
  • Kawano K., Hamasaki N. Isolation of a 5300-Dalton peptide containing a pyridoxal phosphate binding site from the 38 000-Dalton domain of band 3 of human erythrocyte membranes. Journal of Biochemistry (Tokyo) 1986; 100: 191–199
  • Kratzin H. D., Wiltfang J., Karas M. M. N., Hilschmann N. Gas-phase sequencing after electroblotting on polyvinylidene difluoride membranes assigns correct molecular weights to myoglobin molecular weight markers. Analytical Biochemistry 1989; 183: 1–8
  • Laemmli U. K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
  • Litman B. Rhodopsin: its molecular substructure and phospholipid interactions. Photochemistry and Photobiology 1979; 29: 671–677
  • Lowry O. H., Roseborough N. J., Farr A. L., Randall R. J. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 1951; 193: 265–275
  • Macara I. A., Kuo S., Cantley L. C. Evidence that inhibitors of anion exchange induce a conformational change in band 3. Journal of Biological Chemistry 1983; 258: 1785–1792
  • Oikawa K., Lieberman D. M., Reithmeier R. A. F. Conformation and stability of the anion transport protein of human erythrocyte membranes. Biochemistry 1985; 24: 2843–2848
  • Okubo K., Kang D., Hamasaki N., Jennings M. L. Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS molecule. Journal of Biological Chemistry 1994; 269: 1918–1926
  • Olmsted J. B. Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. Journal of Biological Chemistry 1981; 256: 11955–11957
  • Pimplikar S. W., Reithmeier R. A. F. Affinity chromatography of band 3, the anion transport protein of erythrocyte membranes. Journal of Biological Chemistry 1986; 261: 9770–9778
  • Poole R. C., Halestrap P. Identification and partial purification of the erythrocyte L-lactate transporter. Biochemical Journal 1992; 283: 855–862
  • Ramjeesingh M., Gaarn A., Rothstein A. The localization of a disulfonic stilbene binding site in band 3, the anion transport protein of the red blood cell membrane. Biochimica et Biophysica Acta 1980; 599: 127–139
  • Rao A., Martin P., Reithmeier R. A. F., Cantley L. C. Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer. Biochemistry 1979; 18: 4505–4516
  • Reithmeier R. A. F. The erythrocyte anion transporter (band 3). Current Opinion in Structural Biology 1993; 3: 515–523
  • Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry 1987; 166: 368–379
  • Tanner M. J. A. Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Seminars in Hematology 1993; 30: 34–57
  • Teufel M., Pompejus M., Humbel B., Friedrich K., Fritz H.-J. Properties of bacteriorhodopsin derivatives constructed by insertion of an exogenous epitope into extramembrane loops. EMBO Journal 1993; 12: 3399–3408
  • Wang D. N., Kuhlbrandt W., Sarabia V. E., Reithmeier R. A. F. Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO Journal 1993; 12: 2233–2239
  • Wang D. N., Sarabia V. E., Reithmeier R. A. F., Kuhlbrandt W. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3. EMBO Journal 1994; 13: 3230–3235
  • Wojcicki W. E., Beth A. H. Structural and binding properties of the stilbenedisulfonate sites on erythrocyte band 3: an electron paramagnetic resonance study using spin labelled stilbenedisulfonates. Biochemistry 1993; 32: 9454–9464
  • Wood P. G., Miiller H., Sovak M., Passow H. Role of lys 558 and lys 869 in substrate and inhibitor binding to the murine band 3 protein: a study of the effects of site-directed mutagnenesis of the band 3 protein expressed in the oocytes of Xenopus laevis. Journal of Membrane Biology 1992; 127: 139–148

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