Purified, haemoglobin-free oxymyoglobin preparations, obtained from heart tissue of adult subjects (Mb A) were compared with myoglobin obtained from heart tissue of fetuses (Mb F) and of individuals with homozygous β-thalassaemia (Mb C). It was found that myoglobin from individuals suffering from homozygous β-thalassaemia was different from that of fetuses and adults. Electrophoretic studies, particularly on acrylamide gel and on cellulose acetate, showed characteristic differences of the components. Two-dimensional peptide maps (fingerprints) showed the presence of a new peptide in Mb C, which was not found in Mb A and Mb F. It appears that the presence of this peptide is associated with a characteristic change in the structure of the Mb C molecule.

Keywords:
Haemoglobin, Mediterranean anaemia, Myoglobin, Thalassaemia
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© 1974 S. Karger AG, Basel
1974
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