Hæmoglobin Types in Ox and Buffalo

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STUDIES of ox and buffalo hæmoglobins by the technique of electrophoresis have been made by several workers. Geiger1, using a technique of cataphoresis, resolved ox hæmoglobin into a component moving anodally and a component moving cathodally at a neutral reaction, and noticed that the two components had different oxygen-dissociation properties. Reiner, Moore, Lang and Green2 and Munro and Munro3, using the moving-boundary technique, resolved ox hæmoglobin into two components at an acid reaction. Using paper electrophoresis, Cabannes and Serain4 found two varieties of hæmoglobin (which they called α and β) in 270 samples of North African oxen (α alone in 76.3 per cent, α plus β in 20.7 per cent, α alone in 4.0 per cent). Giri and Pillai5 studied buffalo hæmoglobin on agar electrophoresis and resolved it into two components.

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  1. 1

    Geiger, A., Proc. Roy. Soc., B, 107, 368 (1930).

  2. 2

    Reiner, L., Moore, D. H., Lang, E. H., and Green, M., J. Biol. Chem., 146, 583 (1942).

  3. 3

    Munro, M. P., and Munro, F. L., J. Biol. Chem., 150, 427 (1943).

  4. 4

    Cabannes, R., and Serain, C., C.R. Soc. Biol., Paris, 149, 7, 1193 (1955).

  5. 5

    Giri, K. V., and Pillai, N. C., Nature, 178, 1057 (1956).

  6. 6

    Chernoff, A. I., New Engl. J. Med., 253, 322 (1955).

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VELLA, F. Hæmoglobin Types in Ox and Buffalo. Nature 181, 564–565 (1958) doi:10.1038/181564a0

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