Structure and function of a new hemoglobin variant, Hb meilahti (alpha 2 beta 2 36(C2)Pro----Thr), characterized by mass spectrometry.
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/z1278 which corresponded to the mass number of the protonated molecular ion of beta T4 with 36Pro----Thr substitution. The structure was confirmed by the mass spectrum of the chymotryptic digest.
D014644:Genetic Variation; D006454:Hemoglobins / Q000235:genetics*; D006455:Hemoglobins, Abnormal / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D010100:Oxygen / Q000097:blood; D011086:Polycythemia / Q000097:blood; D013329:Structure-Activity Relationship
D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; C042854:hemoglobin Linkoeping; D010100:Oxygen