Abstract
SINCE the first haemoglobin G was described in 1954 (ref. 1), several varieties have been observed. Structural analysis has shown that the electrophoretic mobility could be due to various amino-acid substitutions in the α- as well as in the β-chain. The only similarity between all these haemoglobins is that the net charge differs from that of normal haemoglobin and that they migrate close to haemoglobin S, but a little faster in alkaline buffer.
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LABIE, D., SCHAPIRA, G. New Variant of Haemoglobin G, Haemoglobin GParis. Nature 209, 1033–1034 (1966). https://doi.org/10.1038/2091033a0
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DOI: https://doi.org/10.1038/2091033a0
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