Abstract
THE equation deduced by Drs. Falk, Phillips and Perrin would seem applicable only when interaction between the ‘metal’ and ligand would be high, for example, in the hæm compounds which have reacted with oxygen or carbon monoxide. If the interaction were low, as it seems to be in the hæmatin compounds on which my experiments were performed, where dissociations appear to be simple (for example, in hydroxide formation) and the linkages ‘essentially ionic’, then the second and third terms on the right-hand side of the equation could be discarded. My interpretation assumed this, and that removal of the insoluble hæmatin, with polymerization and loss of absorbance, ‘indicated’ the dissociation of the bonding group of the protein. It was also assumed that over the range of hydrogen ion concentration studied, contributions to the absorbance from linkages to the hæmatin propionate side-chains would be low. The latter opinion now appears confirmed, since the dissociation of ferriætiomyoglobin (prepared from ætiohæmin, with no carboxyl groups) apparently follows the theoretical curve for an acid group with pK = 4.95 (at 21°, µ = 0.05)1.
Similar content being viewed by others
Article PDF
References
O'Hagan, J. E., paper read at symposium on Hæmatin Enzymes, arranged by Aust. Acad. Sci., Canberra, Aug. 31–Sept. 4, 1959.
Cohn, E. J., Green, A. A., and Blanchard, M. H., J. Amer. Chem. Soc., 59, 509 (1937).
Keilin, J., Biochem. J., 49, 544 (1941).
Haurowitz, F., and Hardin, R. L., in “The Proteins”, edit. Neurath, H., and Bailey, K., 2, 332 (1954). Haurowitz, F. (private communication, 1959).
Theorell, H., and Ehrenberg, A., Acta Chem. Scand., 5, 823 (1951). George, P., ‘Currents in Biochemical Research’, 338 (Intersci. Pub. Inc., N.Y., 1956).
German, B., and Wyman, J., J. Biol. Chem., 117, 535 (1937).
Wyman, J., J. Biol. Chem., 127, 581 (1939).
Ferry, R. M., and Green, A. A., J. Biol. Chem., 81, 175 (1929).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
O'HAGAN, J. Banding of Hæm to Protein in Hæmoglobin and Myoglobin. Nature 184, 1652 (1959). https://doi.org/10.1038/1841652a0
Issue Date:
DOI: https://doi.org/10.1038/1841652a0
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.