Abstract
THE following hæmoglobins from human blood are known at present: normal adult (A), fœtal (F), sickle cell (B), and C, D, E and G. The most useful method of distinguishing between these hæmoglobins is based on their different electrophoretic mobilities, while some of them also have other characteristic properties such as high resistance to alkali (F) and low solubility (B). The amino-acid composition of the different hæmoglobins has been discussed in recent years; thus Schroeder et al. 1 found that the amino-acid composition of carboxyhæmoglobin-A and B was about the same, and van der Linden2 described differences in the amino-acid composition of globins prepared from blood of normal adults and from cord blood3.
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References
Schroeder, W. A., Kay, L. M., and Wells, I. C., J. Biol. Chem., 187, 221 (1950).
Linden, A. C. van der, thesis, Amsterdam (1949).
Dustin, J. P., Schapira, G., Dreyfus, J. C., and Hestermans-Medard, O., C.R. Soc. Biol., 148, 1207 (1954).
Chernoff, A. I., Blood, 8, 399 (1953).
Moore, S., and Stein, W. H., J. Biol. Chem., 211, 893 (1954).
Schaaf, P. C. van der, and Huisman, T. H. J., Biochim. Biophys. Acta (in the press).
Zinsser, H. H., Arch. Biochem. and Biophys., 38, 195 (1952).
Itano, H. A., and Neel, J. V., Proc. U.S. Nat. Acad. Sci., 36, 613 (1950).
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HUISMAN, T., JONXIS, J. & SCHAAF, P. Amino-Acid Composition of Four Different Kinds of Human Hæmoglobin. Nature 175, 902–903 (1955). https://doi.org/10.1038/175902a0
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DOI: https://doi.org/10.1038/175902a0
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