Abstract
A survey of blood specimens from 146 American bison, Bison bison, showed the presence of two hemoglobin phenotypes because the ratio of the two normally occurring hemoglobins differed. These two hemoglobins, which are readily identified by their electrophoretic properties and are referred to as Hb-fast and Hb-slow, have been found in all bison. Chromatographic analyses showed that in the majority of animals the ratio between the relative amounts of Hb-fast and Hb-slow was about 60:40, but in three animals from South Dakota this ratio was about 80:20. Structural studies were made on the α chains of Hb-fast and Hb-slow from one animal with the 60:40 ratio and on those from a second animal with the 80:20 ratio. Four types of α chains could be demonstrated which differ from each other by at least one to three amino acid residues. It is suggested that these four α-chain types are the products of two nonallelic Hb α structural genes and their alleles.
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Abe, T., Oishi, T., and Suzuki, S. (1969). Hemoglobin, transferrin, and albumin variants in Formosan water buffalo. Proc. Japan Acad. 45767.
Adams, H. R., Wrightstone, R. N., Miller, A., and Huisman, T. H. J. (1969). Quantitation of hemoglobin α chains in adult and fetal goats: Gene duplication and the production of polypeptide chains. Arch. Biochem. Biophys. 132223.
Anson, M. L., and Mirsky, A. E. (1930). Protein coagulation and its reversal. The preparation of insoluble globin, soluble globin and heme. J. Gen. Physiol. 13469.
Babin, D. R., Schroeder, W. A., Shelton, J. R., Shelton, J. B., and Robberson, B. (1966). The amino acid sequence of the γ chain of bovine fetal hemoglobin. Biochemistry 51297.
Balini, A. S., and Barnabas, J. (1965). Polypeptide chains of buffalo haemoglobins. Nature 2051019.
Braend, M., and Gasparski, J. (1967). Haemoglobins and transferrin of European bison and their cattle hybrids. Nature 21498.
Braend, M., and Stormont, C. (1963). Haemoglobin and transferrin types in the American buffalo. Nature 197910.
Clegg, J. B., Naughton, M. A., and Weatherall, D. J. (1966). Abnormal human hemoglobins. 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. Mol. Biol. 1991.
Dozy, A. M., Kleihauer, E. F., and Huisman, T. H. J. (1968). Studies on the heterogeneity of hemoglobin. XIII. Chromatography of various human and animal hemoglobin types on DEAE-Sephadex. J. Chromatogr. 32723.
Efremov, G. D., Huisman, T. H. J., Smith, L. L., Wilson, J. B., Kitchens, J. L., Wrightstone, R. N., and Adams, H. R. (1969). Hemoglobin Richmond, a human hemoglobin which forms asymmetric hybrids with other hemoglobins. J. Biol. Chem. 2446105.
Huisman, T. H. J., Brandt, G., and Wilson, J. B. (1968). The structure of goat hemoglobins. II. Structural studies of the α chains of the hemoglobins A and B. J. Biol. Chem. 2433675.
Ranjekar, R. K., and Barnabas, J. (1969). Hemoglobin phenotypes in water buffalo (Bos bubalus) during development. Comp. Biochem. Physiol. 281395.
Schroeder, W. A., and Robberson, B. (1965). An improved gradient for ion exchange chromatography of peptides on Dowex 1. Anal. Chem. 371583.
Schroeder, W. A., Jones, R. T., Cormick, J., and McCalla, K. (1962). Chromatographic separation of peptides on ion exchange resins. Separation of peptides from enzymatic hydrolysates of the α, β, and γ chains of human hemoglobins. Anal. Chem. 341570.
Schroeder, W. A., Shelton, J. R., Shelton, J. B., Cormick, J., and Jones, R. T. (1963). The amino acid sequence of the γ chain of human fetal hemoglobin. Biochemistry 2992.
Schroeder, W. A., Shelton, J. R., Shelton, J. B., Robberson, B., and Babin, D. R. (1967). Amino acid sequence of the α-chain of bovine fetal hemoglobin. Arch. Biochem. Biophys. 1201.
Vella, F. (1958). Haemoglobin types in ox and buffalo. Nature 181564.
Wilson, J. B., Brandt, G., and Huisman, T. H. J. (1968). The structure of sheep hemoglobins. III. Structural studies of the α chain of hemoglobin A. J. Biol. Chem. 2433687.
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This research was supported by United States Public Health Service Research Grant HL-05168.
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Harris, M.J., Wilson, J.B. & Huisman, T.H.J. Two hemoglobin phenotypes in the American bison (Bison bison): A possible genetic explanation based on structural studies. Biochem Genet 9, 1–11 (1973). https://doi.org/10.1007/BF00485586
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DOI: https://doi.org/10.1007/BF00485586