Summary
The existence of embryonic hemoglobins is demonstrated in sheep-, calf and pig embryos. The occurrence and disappearance of these hemoglobins is quantitatively determined by cellulose acetate gel electrophoresis; hemoglobins as well as the globin chains, dissociated in 8 molar urea were quantitated. Sedimentation and diffusion experiments in the analytical ultracentrifuge revealed a S20 of 4.3 and a D20 of 6.6 for the examined hemoglobins. Therefore it is concluded that all hemoglobins occurring at different stages of embryonic and fetal development consist of 4 polypeptide chains with a total molecular weight of 66,000. The subsequent formation of the different polypeptide chains during ontogenesis is shown: At first only ε-chains are formed as demonstrated by the existence of Hb Gower I, consisting of four identical ε-chains. Subsequently the α-chain appears, which leads to Hb Gower 2 (α2ε2). The third polypeptide chain formed during the ontogenesis the γ-chain results finally in the appearance of HbF.
In addition the existence of a HbF pig is demonstrated by the fingerprint technique.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Archibald, W. J.: A demonstration of some new methods of determining molecular weights from the data of the ultracentrifuge. J. Phys. Colloid Chem. 51, 1204 (1947).
Aronsson, T., and A. Grönwall: Improved separation of serum proteins in paper electrophoresis: A new electrophoresis buffer. Scand. J. clin. Lab. Invest. 9, 338 (1957).
Babin, D. R., W. A. Schroeder, R. J. Shelton, J. B. Shelton, and B. Robberson: The amino acid sequence of the γ-chain of bovine fetal hemoglobin. Biochemistry 5, 1297 (1966).
Betke, K., u. E. Kleihauer: Fetaler und bleibender Blutfarbstoff in Erythrocyten und Erythroblasten von menschlichen Feten und Neugeborenen. Blut 4, 241 (1958).
Capp, G. L., D. A. Rigas, and R. T. Jones: Hemoglobin Portland 1: A new human hemoglobin unique in structure. Science 157, 65 (1967).
Clegg, J. B., M. A. Naughton and D. J. Weatherall: Abnormal human haemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. molec. Biol. 19, 91–108 (1966).
Elias, H. C.: Theorie und Praxis der Ultrazentrifugentechnik. München: Beckman Instruments 1961.
Gratzer, W. B., and A. C. Allison: Multiple haemoglobins. Biol. Rev. 35, 459 (1960).
Hecht, F., A. G. Motulsky, R. J. Lemire, and Th. E. Shepard: Predominance of hemoglobin Gower I in early human embryonic development. Science 152, 91 (1966).
Hill, R. J., and L. C. Craig: Counter current distribution studies with adult human hemoglobin. J. Am. chem. Soc. 81, 2272 (1959).
Huehns, E. R., N. Dance, G. H. Beaven, J. V. Kell, F. Hecht, and A. G. Motulsky: Human embryonic hemoglobins. Nature (Lond.) 201, 1095–1097 (1964).
—, F. Hecht, J. V. Keil, and A. G. Motulsky: Developmental hemoglobin anomalies in a chromosomal triplication: D 1 trisomy syndrome. Proc. nat. Acad. Sci. (Wash.) 51, 89–97 (1964).
Kabat, D., and G. Attardi: Synthesis of chicken hemoglobins during erythrocyte differentiation. Biochim. biophys. Acta (Amst.) 138, 382 (1967).
Kaltsoya, A., P. Fessas, and A. Stavropoulos: Hemoglobins of early human embryonic development. Science 153, 1417–1418 (1966).
Kleihauer, E.: Spectral properties of normal and abnormal hemoglobins. XI. Congr. Int. Soc. Haemat., Sydney 1966.
—, D. Tang u. K. Betke: Die intrazelluläre Verteilung von embryonalem Hämoglobin in roten Blutzellen menschlicher Embryonen. Ein Beitrag zur Ontogenese menschlicher Hämoglobine. Acta haemat. (Basel) 38, 264 (1967).
Kunkel, H. G., and G. Wallenius: New haemoglobin in normal adult blood. Science 122, 288 (1955).
Rossi Fanelli, A., E. Antonini, and A. Caputo: Studies on the structure of hemoglobin. I. Physicochemical properties of human globin. Biochim. biophys. Acta (Amst.) 30, 608 (1958).
Schachmann, H. K.: In: Ultracentrifugation, diffusion and viscosimetry. In: Methods in enzymology, vol. IV. New York: Academic Press 1957.
Schroeder, W. A., J. R. Shelton, J. B. Shelton, B. Robberson, and D. R. Babin: Amino acid sequence of the α-chain of bovine fetal hemoglobin. Arch. Biochem. 120, 1–14 (1967).
Streeter, G. L.: Cit in Biology data book, ed. Altman and Dittmer: Federation of American Societies for Experimental Biology.
Teale, F. W. J.: Cleavage of the haem-protein link by acid methylethylketone. Biochim. biophys. Acta (Amst.) 35, 543 (1959).
Wilson, J. B., W. C. Edwards, M. McDaniel, M. M. Dobbs, and T. H. I. Huisman: The structure of sheep hemoglobins. II. The amino acid composition of the tryptic peptides of the non-α chains of hemoglobins A, B, C and F. Arch. Biochem. 115, 385 (1966).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kleihauer, E., Stöffler, G. Embryonic hemoglobins of different animal species. Molec. Gen. Genet. 101, 59–69 (1968). https://doi.org/10.1007/BF00434812
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00434812