Abstract
IT was shown by Zeynek1 that on drying deoxygenated hæmoglobin in vacuo at 40°, its characteristic one-banded absorption spectrum is replaced by that of a hæmochromogen with two bands at 556 and 528 mµ, the first band being much stronger than the second. On re-introducing water containing oxygen, the absorption spectrum of the hæmochromogen is rapidly replaced by that of oxyhæmoglobin. These important observations were recently confirmed and extended by Haurowitz2, who put forward the view that the formation of this anhydro-hæmoglobin is due to the removal of the water molecule occupying the sixth co-ordination bond of the iron atom, followed by polymerization of the resulting products, in which the iron of one is linked with the protein of another.
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References
Zeynek, R., Noviny Lekarskie, Poznan, 38, 406 (1926).
Haurowitz, F., “Hæmoglobin, a Symposium in Memory or Sir Joseph Barcroft”, 53 (Butterworth, London, 1949).
Haurowitz, F., J. Biol. Chem., 193, 443 (1951).
Keilin, D., and Hartree, E. F., Nature, 164, 254 (1949).
Coryell, C. D., Stitt, F., and Pauling, L., J. Amer. Chem. Soc., 59, 633 (1937).
Anson, M. L., and Mirsky, A. E., J. Gen. Physiol., 14, 725 (1931); 17, 399 (1934).
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KEILIN, D., HARTREE, E. Effect of Drying upon the Absorption Spectra of Hæmoglobin and its Derivatives. Nature 170, 161–162 (1952). https://doi.org/10.1038/170161a0
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DOI: https://doi.org/10.1038/170161a0
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