Letter | Published:

Sedimentation Characteristics of the Human Hæmoglobins A, F and E

Naturevolume 199pages919920 (1963) | Download Citation

Subjects

Abstract

IT is now well established that normal human hæmoglobin A consists of four polypeptide chains of two types named α and β (ref. 1). The normal foetal hæmoglobin F also consist of four polypeptide chains of two types, namely, α and γ (ref. 2). Thus the difference between the Hb-A and Hb-F is the substitution of two complete γ-chains for the two β-chains. A number of physical and chemical differences between these two hæmoglobins have been discovered3 which are undoubtedly associated with this replacement. However, no systematic study of difference, if any, in the sedimentation character of these two hæmoglobins appears to have been made as most of the previous sedimentation studies were concerned with Hb-A4–8. This communication describes comparative investigations of the sedimentation behaviour of two normal human hæmoglobins A and F. When the measurements were in progress, samples of pure hæmoglobin E were available from the blood of a homozygous subject (E. E.), whose blood contained 98 per cent Hb-E and 2 per cent Hb-F. Some sedimentation studies were also carried out with this abnormal human hæmoglobin E, which differs from hæmoglobin A by the replacement of a single amino-acid, glutamic acid, by lysine in the 26th residue of the β-chain9. No previous sedimentation examination of Hb-E has been carried out.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Rhinesmith, H. S., Schroeder, W. A., and Martin, N. J., J. Amer. Chem. Soc., 80, 3358 (1958).

  2. 2

    Schroeder, W. A., and Matsuda, G., J. Amer. Chem. Soc., 80, 1521 (1958).

  3. 3

    White, J. C., and Beaven, G. H., Brit. Med. Bull., 15, 33 (1959).

  4. 4

    Kegeles, G., and Gutter, F. J., J. Amer. Chem. Soc., 73, 3770 (1951).

  5. 5

    Field, E. O., and O'Brien, J. R. P., Biochem. J., 60, 656 (1955).

  6. 6

    Gutter, F. J., Sober, H. A., and Peterson, E. A., Arch. Biochem. Biophys., 62, 427 (1956).

  7. 7

    Rossi-Fanelli, A., Antonini, E., and Caputo, A., J. Biol. Chem., 236, 391 (1961).

  8. 8

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

  9. 9

    Hunt, J. A., and Ingram, V. M., Nature, 184, 870 (1959).

  10. 10

    Singer, K., Chernoff, A. F., and Singer, L., Blood, 6, 429 (1951).

  11. 11

    Donaldson, R., Sisson, R. B., King, E. J., Wooton, I. D. P., and Mac-farlane, R. G., Lancet, i, 874 (1951).

  12. 12

    Hill, R. J., Konigsberg, W., Guidotti, G., and Craig, L. C., J. Biol. Chem., 237, 1549 (1962).

  13. 13

    Braunitzer, G., Gehring-Muller, R., Hilschmann, N., Hilse, K., Hobom, G., Rudloff, V., and Wittmann-Liebold, B., Hoppe-Seyl. Z., 325, 283 (1961).

  14. 14

    Cullis, A. F., Muirhead, H., Perutz, M. F., Rossmann, M. G., and North, A. C. T., Proc. Roy. Soc., A, 265, 161 (1962).

  15. 15

    Field, E. O., and Ogston, A. G., Biochem. J., 60, 661 (1955).

Download references

Author information

Affiliations

  1. Biophysics Division, Saha Institute of Nuclear Physics, Calcutta

    • PANKAJ GANGULY
    • , N. N. DAS GUPTA
    •  & J. B. CHATTERJEA
  2. Hæmatology Department, School of Tropical Medicine, Calcutta

    • PANKAJ GANGULY
    • , N. N. DAS GUPTA
    •  & J. B. CHATTERJEA

Authors

  1. Search for PANKAJ GANGULY in:

  2. Search for N. N. DAS GUPTA in:

  3. Search for J. B. CHATTERJEA in:

About this article

Publication history

Issue Date

DOI

https://doi.org/10.1038/199919a0

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.