Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Structure and function of isolated components.
Four major components of the hemoglobin of the bullfrog tadpole, Rana catesbeiana, have been isolated and characterized structurally and functionally. These components fall into two clear functional classes. Components I and II have substantially higher affinities for oxygen than do components III and IV. Components I and II predominate in very young tadpoles and are largely replaced by components III and IV in older tadpoles. The data (Broyles, R.H., and Frieden, E. (1973) Nature New Biol. 241, 207-209) indicate that component I arises in the kidney and components III and IV in the liver. The synchrony of appearance and functional similarity o components I and II suggest that component II probably also arises in the kidney. Thus the development of the tadpole is associated with the successive proliferation of three distinct populations of red cells, first from the kidney, then from the liver, and finally, after metamorphosis, from bone marrow...
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002248:Carbon Monoxide / Q000097:blood; D002268:Carboxypeptidases; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008675:Metamorphosis, Biological; D010100:Oxygen / Q000097:blood; D010108:Oxyhemoglobins; D010446:Peptide Fragments / Q000032:analysis / Q000502:physiology; D011892:Rana catesbeiana / Q000097:blood*; D013997:Time Factors; D014357:Trypsin
D000596:Amino Acids; D006454:Hemoglobins; D010108:Oxyhemoglobins; D010446:Peptide Fragments; D002248:Carbon Monoxide; D002268:Carboxypeptidases; D014357:Trypsin; D010100:Oxygen