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The hemoglobin (hgb) from a patient with Hgb M disease was resolved
into two components by starch block electrophoresis (at pH 7.0-7.2) of the
oxidized hemolyzate. One component was identified electrophoretically and
spectroscopically as Hgb A, and the other as Hgb M. Methods for the determination of the relative concentration of Hgb M were given. In the patient reported, Hgb M was found to comprise approximately 30 per cent of the total
hgb. Spectroscopic studies of electrophoreticably isolated Hgb M demonstrated
that both the methgb and the cyanmethgb form were abnormal in their spectral
curves. The reactions of the methgb form with low and high concentrations
of cyanide were found to differ. The nature of the spectral changes were
such as to indicate that some of the heme groups of the methgb form react
abnormally and others apparently normally. The electrophoretic behavior of
the patient’s hemolyzate after treatment with various combinations of cyanide
and ferricyanide was consistent with this hypothesis. The differing reactivity
of the heme groups was explained in the light of the biochemical genetics of
the abnormal hemoglobins.
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| Copyright © 1958 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
