Concurrent synthesis of two or more hemoglobins occurs in normal man, the human hemoglobinopathies, and certain animal species. Duck erythrocytes produced in response to acutely induced anemic hypoxia (hemolysis or blood loss) contained reciprocally altered proportions of Hb I (alpha(2) (I) beta(2) (I)) and Hb II (alpha(2) (II) beta(2) (II)); the relative proportion of Hb II was 50-100% increas...

Introduction A wide diversity in both structure and function has been discovered in the study of hemoglobins (Hbs) from many species. Hemoglobins play oxygen transport in red blood cells in higher organisms. Even though oxygen molecule can diffuse into the cell, unicellular organisms also have hemoglobin-like molecules [1]. Truncated hemoglobins (trHbs) are distributed from bacteria to unicellu...

By H’ mit si KITCHEN, FRANK W . PUTNAM AND \V. JAPE TAYLOR I HE SICKLING OF ERYTHROCYTES under in vitro laboratory conditions has been demonstrated in most species of deer. This remarkable distortion of the erythrocytes from the biconcave disc shape to such bizarre forms as holly leaf, crescent and oat shapes in several species of deer was first described by Gulliver in 1840. Seventy years late...

The mechanisms of hemoglobin precipitation into Heinz bodies and hemolytic anemia that characterize congenital Heinz body hemolytic anemia (CHBHA) were studied in patients with the unstable hemoglobins, Köln (beta-98 valine --> methionine) and Hammersmith (beta-42 phenylalanine --> serine). The cysteines in the 93rd position of the beta-chains of CHBHA hemoglobins bound glutathione excessively ...

Ultracentrifugation studies on hemolysates from the erythrocytes of the hagfish, Eptatretus burgeri, showed that in dilute solution oxygenated hemoglobins were in a monomeric form with a molecular weight of approximately 18,000. In deoxygenated hemolysates or in concentrated solutions of oxygenated hemolysates, an aggregate product appeared which was considered to be a tetramer, as judged from ...

Hemoglobin is a conjugated protein composed of heme prosthetic groups united to polypeptide chains. The structure, four heme groups associated with four polypeptide chains, seems to be similar for all mammalian hemoglobins (1). Usually the polypeptide chains appear in two forms, which in adults are called a and @ chains. Homology occurs among the polypeptide chains of hemoglobins partially beca...

Circular dichroism (CD) of various kinds of hemoglobins and the protoporphyrin-globin complex has been measured over the range of 200 to 660 nm. All mammalian hemoglobins so far tested show CD spectra identical with those of human hemoglobin. Although the absorption spectra of lamprey hemoglobin and toad embryonic hemoglobin are similar to those of human hemoglobin, these hemoglobins show vario...