Abstract
Neonatal mouse spleens have, in addition to or in place of adult hemoglobin, an electrophoretically fast hemoglobin band. The proportion of this fast-migrating band is increased significantly by gently heating the sample prior to electrophoresis. In contrast, gentle heating of the sample in the presence of Cleland's reagent prior to electrophoresis reduces the proportion of the fast band to near zero. We conclude that the fast band consists of adult-type hemoglobin linked via a disulfide bridge to some small molecule with an overall negative charge, possibly glutathione.
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