Abstract
A new hemoglobin was produced in sheep with Hb A during experimental anemias. This hemoglobin, called Hb Aα, had different electrophoretic characteristics and denatured with alkali at a faster rate than normal Hb A. It also showed electrophoretic differences to Hb B and Hb F. Hb Aα was located almost entirely in the reticulocytes produced during the anemia. The reticulocytes produced in anemic sheep with Hb B contained a hemoglobin which showed only minor differences from the normal hemoglobin on electrophoresis. However, it denatured at a faster rate than the normal hemoglobin. It is postulated that Hb Aα is a relatively unfinished hemoglobin associated with the immature erythrocytes produced after a severe anemic stress. It did not appear to be fetal hemoglobin.
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