Abstract
THE preparation of globin from hæmoglobin by removal of the hæm with acid has long been known1, but it has become increasingly clear that such globin preparations, when recombined with hæm, give a product differing from the original hæmoglobin in some properties such as spectral absorption2 and solubility. Gralén showed3 that although in the ultracentrifuge recombined hæm–globin gave results similar to those of the original horse hæmoglobin, electrophoresis showed up differences.
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References
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Wyman, J., “Advances in Protein Chemistry", 4, 454 (1948). Jope, E. M., in ”Hæmoglobin", papers presented at the Sir Joseph Barcroft Memorial Conference, Cambridge, 1948, p. 218 (London, 1949). Jope, E. M., quoted in Rimington, C., and Fulton, J. D., Biochem. J., 41, 619 (1947).
Gralén, N., Biochem. J., 33, 1907 (1939). It may be noted that free globins appear to have molecular weights of the order 34,000, half that of the red cell hæmoglobins.
Holiday, E. R., J. Sci. Instr., 14, 166 (1937); a more recent account is in the press.
Drabkin, D. L., J. Biol. Chem., 158, 721 (1945).
Jope, E. M., in “Hæmoglobin", papers presented at the Sir Joseph Barcroft Memorial Conference, Cambridge, 1948, p. 216 (London, 1949).
Holiday, E. R., and Jope, E. M. (to be published).
Crammer, J. L., and Neuberger, A., Biochem. J., 37, 302 (1945).
Perutz, M. F., and Weisz, O., Nature, 160, 786 (1947). Jope, H. M., and O'Brien, J. R. P., in “Hæmoglobin", papers presented at the Sir Joseph Barcroft Memorial Conference, Cambridge, 1948, p. 269 (London, 1949).
Compare Thorell, B., Acta med. Scand., Supp., 200, 89 (1947). Dacie, J. V., and White, J. C., J. Clin. Path., 2, 21 (1949).
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JOPE, E., JOPE, H. & O'BRIEN, J. Crystallizable Recombined Hæm-Globin from Human Red-Cell Hæmoglobin. Nature 164, 622–623 (1949). https://doi.org/10.1038/164622b0
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DOI: https://doi.org/10.1038/164622b0
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