Abstract
Summary
Two hemoglobins were obtained from erythrocytes of the adult, male Pekin duck by use of ion-exchange chromatography. The hemoglobins were found to differ in amount within the cells by about 6-fold and in amino acid composition of the constituent globins. The globin corresponding to the minor hemoglobin contains the greater number of amino acid residues, notably those of aspartic plus glutamic acid. The difference between the globins in acid residues may account for the difference in chromatographic behavior of the parent hemoglobins. The relationship between the incorporation of glycine-2-14C and 59Fe into the hemoglobins by erythrocytes in vitro suggest a higher rate but later completion of synthesis for the major hemoglobin than for the other. The ferriforms of the hemoglobins exchange heme in solution but not within the erythrocytes; thus, the hemoglobins may be confined within different cells.
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