Results
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The results of this study indicate that the Brockton variant has no major effect on the oxygen affinity of hemoglobin in blood or hemolysate. This is probably because the replacement of asparagine with proline at beta 138 does not disrupt critical inter and intrahelix hydrogen bonds or salt bridges.
Conclusions
A new unstable hemoglobin variant with Bet decreased intrinsic oxygen affinity has been identified in patients with a mild anemia. Hemoglobin Calais (beta 138(H16) Ala----Pro) is similar to Hb A in electrophoretic mobility and cannot be resolved from Hb A by hemolysate. X-ray crystallographic studies suggest that the substitution disrupts critical inter and intrasubunit hydrogen bonds at beta 138, and that this may be responsible for its instability.
Hemoglobin Brockton is a high linear energy transfer (LET) mutant with a decreased ability to bind large alpha particles. This suggests that it may be a candidate for a therapeutic agent.
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