Abstract
The globins from all fast haemoglobin (Hb) components obtainable by Bio-Rex 70 cation-exchange chromatography were examined by isoelectrofocusing on polyacrylamide gel rods with 8.0 mol/l urea. From this analysis HbA 1a1 and HbA 1a2 seem to be very heterogeneous components. HbA 1b is separable into two components, one of which is varied in both the β chains. Between HbA 1b2 and the well-known HbA 1c components two chromatographic peaks are separated, one with a noticeable percentage of glucosylated β chain and one that probably contains HbF. HbA 1c has both β chains glucosylated, while HbA 1x seems to be a β monoglucosylated Hb form. Finally, the early part of the HbA 0 peak has a large amount of glucosylation on both α and β chains.
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