Letter | Published:

A New Hæmoglobin Variant exhibiting Anomalous Electrophoretic Behaviour

Nature volume 180, pages 14861487 (28 December 1957) | Download Citation



IN moving-boundary electrophoresis, cacodylate buffer, pH 6.5, µ0.1, the relative mobilities of the better-known hæmoglobin variants are the same or only slightly different from those in paper electrophoresis, veronal buffer, pH 8.6, µ0.05. Owing to the fact that the two buffers are on the opposite sides of the isoelectric points of these types of hæmoglobin, the order of migration is reversed; however, the relative mobilities of hæmoglobin types A, S = D and C are identical under both conditions. The earliest instance of a type of hæmoglobin exhibiting some discrepancy in behaviour in free electrophoresis as compared to paper electrophoresis is that of hæmoglobin F; with the latter technique, the mobility of F is always slightly less than that of A, but with the former, F is indistinguishable from A. A somewhat greater difference occurs in the mobility of hæmoglobin E, which, in veronal paper electrophoresis (pH 8.6), lies between S and C, but in free electrophoresis (cacodylate, pH 6.5) is slightly less than that of S (between S and A)1. Similarly, the mobility of hæmoglobin G lies between F and S in paper electrophoresis at pH 8.6; but in free electrophoresis at pH 6.5 (cacodylate) G is inseparable from S2.

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    , , and , J. Amer. Chem. Soc., 76, 2278 (1954).

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    , , and , Nature, 175, 850 (1955).

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    , Texas Rep. Biol. and Med., 14, 380 (1956).

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    , and , , Roy. Soc. Trop. Med. and Hyg., 50, 614 (1956).

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  1. Tissue Metabolism Research Laboratory, University of Texas Medical Branch, Galveston, Texas. Aug. 2.



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