Structure and Function of a New Hemoglobin Variant, Hb Meilahti (α2β2 36(C2)Pro→Thr), Characterized by Mass Spectrometry

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Abstract
An abnormal hemoglobin was found by isoelectric focusing in the blood of a Finnish woman with erythrocytosis. Oxygen equilibrium curves of the patient’s hemolysate indicated the presence of a variant with a very high oxygen affinity. Structural analysis was carried out by mass spectrometry. In the spectrum of the tryptic digest, an abnormal peptide was found at m/zl278 which corresponded to the mass number of the pro-tonated molecular ion of βT4 with 36Pro→Thr substitution. The structure was confirmed by the mass spectrum of the chymotryptic digest

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