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- Title
Structure and Function of a New Hemoglobin Variant, Hb Meilahti (α<sub>2</sub>β<sub>2</sub> 36(C2)Pro→Thr), Characterized by Mass Spectrometry.
- Authors
Wada, Y.; lkkala, E.; Imai, K.; Matsuo, T.; Matsuda, H.; Lehtinen, M.; Hayashi, A.; Lehmann, H.
- 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 Copyright © 1987 S. Karger AG, Basel
- Publication
Acta Haematologica, 1987, Vol 78, Issue 2/3, p109
- ISSN
0001-5792
- Publication type
Article
- DOI
10.1159/000205856