Abstract
Two distinct electrophoretic types of sheep haemoglobin have been identified by Harris and Warren1. They designated the fast-moving component which travelled towards the anode at pH. 8.6 ‘haemoglobin A’, and the slow-moving one ‘haemoglobin B’ Similar electrophoretic differences were found with adult haemoglobins in Dutch sheep by Helm at al.2, which they named HbI and HbII, corresponding to HbB and HbA respectively. Further differences in chromatographic behaviour, in resistance to denaturation by alkali, in solubility in concentrated salt solutions and in amino-acid composition were demonstrated for HbI and HbII2. The oxygen equilibrium curves of these haemoglobins were also found to be different3,4, HbII(A) having a higher affinity for oxygen than Hbl(B), and it has been suggested that HbII(A) originated in sheep living at high altitude.
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