Abstract
THE human embryonic haemoglobins (Hbs) Gower 1 and Gower 2 (ref. 1) are present in fetuses up to 60 mm crown–rump measurement2. However, relatively little is known about the structure and function of these haemoglobins because of the difficulty in obtaining suitable material, particularly since the introduction of the suction method for terminating pregnancy in the first trimester. Here we present the amino acid composition and sequence data for the human e-chain, prepared by purifying Hb-Gower 2 (α2e2) from early abortion samples. In addition, separation of embryonic red cells from the majority of the maternal red cells has led to the isolation of Hb-Gower 1 and the demonstration that it has the composition ζ2e2.
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