Abstract
The nuclear fraction of hemoglobin was obtained from chicken red blood cells by hemolytic procedure and the heterogeneity of this hemoglobin was studied by means of paper electrophoresis.Chicken hemoglobin was separated into two components; main and small components. There was no any significant difference between the migrating patterns of the nuclear and the cytoplasmic fractions of hemoglobin. But in densitometric analysis, there was the increase of main component in nuclear fraction as compared with cytoplasmic fraction. These results suggested that the ghost hemoglobin remained in nuclear fraction after hemolysis is composed of two components, the concentrations of which are different in proportion from those of dissolved cytoplasmic fraction.The supernatant of hemoglobin solution which was dialysed against the saturated ammonium sulphate solution contained main component only, whereas the pellet exhibited two components. It might be supposed that the solubility of chicken hemoglobin, especially the small component, is lowered by sulphate ion.The main and small components showed the absorption spectra characteristic of oxy-hemoglobin and marked trytophan notches.
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