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Mechanism of denaturation of haemoglobin by alkali

Naturevolume 247pages341344 (1974) | Download Citation

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Abstract

Denaturation by alkali is activated by the ionisation of buried, weakly acidic side chains. Species variations are largely accounted for by replacements of one buried tyrosine and two cysteines.

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References

  1. 1

    Perutz, M. F., Murihead, H., Cox, J. M., and Goaman, L. C. G., Nature, 219, 131 (1968).

  2. 2

    Perutz, M. F., Proc. R. Soc., B 173, 113 (1969).

  3. 3

    Haurowitz, F., Z. physiol. Chem., 183, 78 (1929).

  4. 4

    Gottlieb, A. J., Robinson, E. A., and Itano, H. A., Archs, Biochem. Biophys., 118, 693 (1967).

  5. 5

    Hasserodt, U., and Vinograd, J., Proc. natn. Acad. Sci. U.S.A., 45, 12 (1969).

  6. 6

    Rosemeyer, M. A., and Huehns, E. R., J. molec. Biol., 25, 253 (1967).

  7. 7

    Hewitt, J. A., Kilmartin, J. V., Ten Eyck, L. F., and Perutz, M. F., Proc. natn. Acad. Sci. U.S.A., 69, 203 (1972).

  8. 8

    Guidotti, G., Konigsberg, W., and Craig, L. C., Proc. natn. Acad. Sci. U.S.A., 50, 774 (1963).

  9. 9

    Perutz, M. F., and Lehmann, H., Nature, 219, 902 (1968).

  10. 10

    Braunitzer, Gehring-Müller, R., Hilschmann, N., Hilse, K., Hoborn, G., Rudloff, V., and Wittmann-Liebold, B., Z. physiol. Chem., 325, 283 (1961).

  11. 11

    Hill, R. J., and Konigsberg, W., J. biol. Chem., 237, 3151 (1962).

  12. 12

    Konigsberg, W., Goldstein, J., and Hill, R. J., J. biol. Chem., 238, 2028 (1963).

  13. 13

    Schroeder, W. A., Shelton, J. R., Shelton, J. B., and Cormick, J., Biochemistry, 2, 1353 (1963).

  14. 14

    Schroeder, W. A., Shelton, J. R., Shelton, J. B., Robberson, B., and Babin, D. R., Archs. Biochem. Biophys., 120, 1, 124 (1967).

  15. 15

    Tanford, C., Adv. protein Chem., 17, 73 (1962).

  16. 16

    Bucci, E. C., Fronticelli, C., Bellelli, L., Antonini, E., Wyman, J., and Rossi-Fanelli, A., Archs. Biochem. Biophys., 100, 364 (1963).

  17. 17

    Bruice, T. C., Fife, T. H., Bruno, J. J., and Brandon, N. E., Biochemistry, 1, 7 (1962).

  18. 18

    Kekwick, R. A., and Lehmann, H., Nature, 187, 158 (1960).

  19. 19

    Huehns, E. R., Dance, N., Shooter, E. M., Beaven, G. H., and Gratzer, W. B., J. molec. Biol., 4, 329 (1962).

  20. 20

    Jones, R. T., Brimhall, B., and Duerst, M., Atlas of Protein Structure and Sequence (edit. by M. O. Dayhoff) (National Biomedical Research Foundation, Washington, 1972).

  21. 21

    Buettner-Janusch, J., and Twichell, J. B., Nature, 192, 669 (1961).

  22. 22

    Dayhoff, M. O., Atlas of Protein Structure and Sequence (National Biomedical Research Foundation, Washington, 1972).

  23. 23

    Matsuda, G., Maita, T., Watanabe, B., Araya, A., Morokuma, K., Ota, Y., Goodman, M., Barnabas, J., and Prychodko, W., Hoppe-Seylers Z. physiol. Chem., 354 (in the press).

  24. 24

    Matsuda, G., Maita, T., Suzuyama, Y., Setoguchi, M., Ota, Y., Araya, A., Goodman, M., Barnabas, J., and Prychodko, W., Hoppe-Seyler's Z. physiol. Chem., 354 (in the press).

  25. 25

    Matsuda, G., Maita, T., Watanabe, B., Ota, H., Araya, A., Goodman, M., and Prychodko, W., Int. J. peptide protein Res., 5 (in the press).

  26. 26

    Matsuda, G., Maita, T., Ota, H., and Takei, H., Int. J. protein Res., 2, 99 (1970).

  27. 27

    Best, J. H., Flamm, U., and Braunitzer, G., Z. physiol. Chem., 350, 563 (1969).

  28. 28

    Haurowitz, F., Hardin, R. L., and Dicks, M., J. phys. Chem., 58, 103 (1954).

  29. 29

    Ayre, G. M., and Thompson, E. O. P., Aust. J. biol. Sci., 24, 75 (1971).

  30. 30

    Greer, J., and Perutz, M. F., Nature new Biol. 230, 261 (1971).

  31. 31

    Hayashi, A., Stamatoyannopoulos, G., Yoshida, A., and Adamson, J., Nature new Biol., 230, 264 (1971).

  32. 32

    Stamatoyannopoulos, G., and Yoshida, A., Science, N.Y., 166, 1005 (1969).

  33. 33

    Kendrew, J. C., Brookhaven Symp. Biol., 15, 216 (1962).

  34. 34

    Romero-Herrera, A. E., and Lehmann, H., Biochim. biophys. Acta., 278, 62 (1972).

  35. 35

    Dautrevaux, M., Boulanger, Y., Han, K., and Biserte, G., Eur. J. Biochem., 11, 267 (1969).

  36. 36

    Singer, K., Chernoff, A. I., and Singer, L., Blood, 6, 413 (1951).

  37. 37

    Beaven, G. H., Ellis, M. J., and White, J. C., Br. J. Haemat., 6, 1 (1960).

  38. 38

    Smith, D. H., Clegg, J. B., Weatherall, D. J., and Giles, H. M., Nature new Biol., 246, 184 (1973).

  39. 39

    Huisman, T. H. G., Wrightstone, R. N., and Wilson, J. B., Archs. Biochem. Biophys., 153, 850 (1972).

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  1. MRC Laboratory of Molecular Biology, Hills Rd, Cambridge

    • M. F. Perutz

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https://doi.org/10.1038/247341a0

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