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Chemical and Enzymatic Modification of Membrane Proteins and Anion Transport in Human Red Blood Cells

  • H. Passow
  • H. Fasold
  • S. Lepke
  • M. Pring
  • B. Schuhmann
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 84)

Abstract

The paper is introduced by a review of the developments which lead to the suggestion of an involvement of the protein in band 3 (nomenclature of Steck, ref.2) in anion transport across the red cell membrane. Subsequently, it is shown that DIDS and its dihydroderivative H2DIDS, which both played an essential role in the reviewed work, not only combine with the protein in band 3 but also with other membrane constituents. At maximal inhibition 1.1–1.3 molecules of DIDS or H2DIDS are bound per molecule of protein in band 3. Combined treatment with 3h pDIDS and esternai chymotrypsin, pronase or papain demonstrates the existence of peptides in the protein in band 3 which differ with respect to their accessibility or susceptibility to proteolysis. Each enzyme affects the protein differently and produces different changes of anion transport. In contrast to external trypsin which has neither an effect on the protein in band 3 nor on anion transport, internal trypsin splits the protein in band 3 completely. Fragments of 58,000 and 48,000 Daltons remain attached to the membrane while other products of hydrolysis are released into the medium. Anion transport is partially inhibited but continues to exhibit the essential features seen in the intact cell. The described results are compatible with an involvement of some component of the protein in band 3 in anion transport. They show that additional evidence is required to provide more definitive proof of such involvement.

Keywords

Membrane Protein Anion Transport Enzymatic Modification Disulfonic Acid Membrane Constituent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    BENDER, W.W., GARAN, H. and BERG, H.C.: J.Mol. Biol. 58 (1971) 783.PubMedCrossRefGoogle Scholar
  2. 2.
    STECK, T.L.: J.Cell.Biol. 62 (1974) 1.PubMedCrossRefGoogle Scholar
  3. 3.
    TANNER, M.J.A. and BOXER, D.H.: Biochem. J. 129 (1972) 333.PubMedGoogle Scholar
  4. 4.
    JULIANO, R.L. and ROTHSTEIN, A.: Bioehim. Biophys. Acta 249 (1971) 227.CrossRefGoogle Scholar
  5. 5.
    FAIRBANKS, G., STECK, T.L., WALLACH, D.P.H.: Biochemistry 10 (1971) 2606.PubMedCrossRefGoogle Scholar
  6. 6.
    BRETSCHER, M.S.: J.Mol.Biol. 59 (1970) 351.CrossRefGoogle Scholar
  7. 7.
    TRIPLETT, R.B. and CARRAWAY, K.L.: Biochemistry 11 (1972) 2897.PubMedCrossRefGoogle Scholar
  8. 8.
    JULIANO, R.L.: Biochim. Biophys. Acta 300 (1973)341.PubMedGoogle Scholar
  9. 9.
    BRETSCHER, M.S.: Nature 231 (1971) 229.CrossRefGoogle Scholar
  10. 10.
    STECK, R.L.: J. Mol. Biol. 66 (1972) 295.PubMedCrossRefGoogle Scholar
  11. 11.
    SHIN, B.C. and CARRAWAY, K.L.: Biochim. Biophys. Acta 345 (1974) 141.PubMedCrossRefGoogle Scholar
  12. 12.
    PINTO DA SILVA, P., MOSS, P.S., PUDENBERG, H.H.: Exptl. Cell. Res. 81 (1973) 127.CrossRefGoogle Scholar
  13. 13.
    KIEPER, H. LINDSTROM, J., LENNA, E.S., SINGER, S.J.: Proc. Nat. Acad. Sci. U.S.A. 67 (1970) 1688.CrossRefGoogle Scholar
  14. 14.
    BELLHORN, M., BLUMENFELD, O.O., GOLLOP, P.M.: Biochem. Biophys. Res. Comm. 39 (1970) 267.PubMedCrossRefGoogle Scholar
  15. 15.
    NICOLSON, G.L. and PAINTER, R.G.: J. Cell Biol. 59 (1973) 395.PubMedCrossRefGoogle Scholar
  16. 16.
    PINTO DA SILVA, P. and NICOLSON, G.L.: Bioehim. Biophys. Acta 363. (1974) 311.CrossRefGoogle Scholar
  17. 17.
    BROWN, P.A., FEINSTEIN, M.B., SHA’AFI, R.I.: Nature New Biol.: 254 (1975) 523.CrossRefGoogle Scholar
  18. 18.
    PINTO DA SILVA, P.: Proc. Nat. Acad. Sci. U.S.A. 70 (1973) 1339.CrossRefGoogle Scholar
  19. 19.
    TAVERNA, R.D. and LANGDON, R.G.: Biochem. Biophys. Res. Comm. 54 (1973) 593.PubMedCrossRefGoogle Scholar
  20. 20.
    LIN, S. and SPUDICH, H.A.: Biochem. Biophys. Res. Comm. 61 (1975) 1471.CrossRefGoogle Scholar
  21. 21.
    Suggested by A. ROTHSTEIN, personal communication.Google Scholar
  22. 22.
    CABANTCHIK, Z.I. and ROTHSTEIN, A.: J. Membrane Biol. 15 (1974) 207.CrossRefGoogle Scholar
  23. 23.
    PASSOW, H., PASOLD, H. ZAKIL, SCHUHMANN, B. and LEPKE, S. In: Biomembranes, Structure and Function (G. Gárdos and I. Szász Edts.) p. 197–214 (Proceedings of the 9th FEBS Meeting, Budapest 1974).Google Scholar
  24. 24.
    PASSOW, H.: Progress in Biophys., Mol. Biol. 19 (1969) 424.Google Scholar
  25. 25.
    POENSGEN, J. and PASSOW, H.: J. Membrane Biol. 6 (1971) 210.CrossRefGoogle Scholar
  26. 26.
    SCHNELL, K.F. and PASSOW, H.: Experientia 25 (1969) 460.PubMedCrossRefGoogle Scholar
  27. 27.
    ZAKI, L., GITLER, C. and PASSOW, H.: XXV Internat. Congress Physiol. Sci. Munich 1971, p. 616.Google Scholar
  28. 28.
    PASSOW, H.: J. Membrane Biol. 6 (1974) 233.CrossRefGoogle Scholar
  29. 29.
    SCHWOCH, G., RUDLOFF, V., WOOD-GUTH, I. and PASSOW, H.: Biochim. Biophys. Acta 339 (1974) 126.PubMedCrossRefGoogle Scholar
  30. 30.
    KNAUF, P.A. and ROTHSTEIN, A.: J.Gen.Physiol. 58 (1971) 19o.Google Scholar
  31. 31.
    OBAID, A.L., REGA, A.F., GARRAHAN, P.: J.Membrane Biol. 9 (1972) 385.CrossRefGoogle Scholar
  32. 32.
    MADDY, A.H.: Biochim. Biophys. Acta 88 (1964) 390.PubMedGoogle Scholar
  33. 33.
    CABANTCHIK, Z.I. and ROTHSTEIN, A.: J. Membrane Biol, 10 (1972) 311.CrossRefGoogle Scholar
  34. 34.
    ZAKI, L., FASOLD, H., SCHUHMANN, B. and PASSOW, H.: J. Cell. Physiol. 86 (1975) 471.PubMedCrossRefGoogle Scholar
  35. 35.
    ROTHSTEIN, A. et al. J. Biol. Chem. In the press.Google Scholar
  36. 36.
    HO, M.K. and GUIDOTTI, G.: J. Biol. Chem. 250 (1975) 675.PubMedGoogle Scholar
  37. 37.
    ROTHSTEIN, A., CABANTCHIK, Z.I., BALSHIN, M. and JULIANO, R.: Biochem. Biophys. Res. Comm. 64 (1975) 144.PubMedCrossRefGoogle Scholar
  38. 38.
    FASOLD, H.: unpublished results.Google Scholar
  39. 39.
    LEPKE, S. and PASSOW, H.: Biochim. Biophys. Acta 298 (1973) 529.PubMedCrossRefGoogle Scholar
  40. 40.
    GUNN, R.B. In; Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status (Rørrth, M. and Astrup Edts.) p. 823–827 Copenhagen, Munksgaard (1972).Google Scholar
  41. 41.
    DALMARK, M.: J. Physiol. (Lond.) 250 (1975) 65.Google Scholar
  42. 42.
    LEPKE, S., FASOLD, H., PRING, M. and PASSOW, H.: J. Membrane Biol., in the press.Google Scholar
  43. 43.
    LÄUGER, P.: Science 178 (1972) 24.PubMedCrossRefGoogle Scholar
  44. 44.
    CABANTCHIK, Z.I. and ROTHSTEIN, A.: J. Membrane Biol. 15 (1974) 227.CrossRefGoogle Scholar
  45. 45.
    STECK, T.L., RAMOS, B. and STRAPAZON, E.: Biochemistry 15 (1976) 1154.CrossRefGoogle Scholar
  46. 46.
    STECK, T.L. and FOX, C.F.: In: Membrane Molecular Biology (Fox, C.F. and Keith, A.D. Edts.) p. 27 Stamford, Conn. Sinauer Assoc. (1972).Google Scholar
  47. 47.
    SCHWOCH, G. and PASSOW, H.: Mol. Cell. Biochem. 2 (1973) 197.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • H. Passow
    • 1
  • H. Fasold
    • 1
  • S. Lepke
    • 1
  • M. Pring
    • 1
  • B. Schuhmann
    • 1
  1. 1.Max-Planck-Institut für Biophysik and Biochemisches InstitutUniversität Frankfurt/MGermany

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