Abstract
Forty-five adult hemoglobin molecular forms which include 22 electrophoretically silent forms were structurally characterized from animal species of nine genera belonging to family Bovidae. Of the 12 different bovid species studied, 11 showed either α or β chain heterogeneity in their hemoglobins while eight species showed heterogeneity for both polypeptide chains. Wherever possible, the genetic basis for hemoglobin phenotypes has been suggested. By construction of a phylogenetic tree for 14 ungulate α-globin sequences, the evolutionary origins of duplicated α chain genes present in some ungulate species have been located, and the phyletic relationship of bovids based on the α globin data is discussed.
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Abe, T., Oishi, T., and Suzerki, S. (1969). Hemoglobin, transferrin and albumin variants in Formosan water buffalo. Proc. Jpn. Acad. 45767.
Adams, H. R., Boyd, E. M., Wilson, J. B., Miller, A., and Huisman, T. H. J. (1968). Structure of goat hemoglobins: Hemoglobin D, a β variant with one apparent amino acid substitution. Arch. Biochem. Biophys. 127398.
Balani, A. S., and Barnabas, J. (1964). Evaluation of multiple hemoglobins of ruminants by tryptic peptide pattern analysis. Ind. J. Biochem. 1220.
Balani, A. S., and Barnabas, J. (1965). Polypeptide chains of buffalo hemoglobins. Nature 2051019.
Barnabas, J., and Muller, C. J. (1962). Hemoglobin Lepore Hollandia. Nature 194931.
Braend, M., and Stormont, C. (1963). Hemoglobin and transferrin types in the American buffalo. Nature 197910.
Braunitzer, G., and Matsuda, G. (1963). Primary structure of α-chains from horse hemoglobin. J. Biochem. 53262.
Chernoff, A. I., and Pettit, N. M. (1964). The amino acid composition of hemoglobin. III. A quantitative method for identifying abnormalities of the polypeptide chains of hemoglobins. Blood 24750.
Clegg, J. B., Naughton, M. A., and Weatherall, D. J. (1966). Separation and characterisation of the α- and β-chains by chromatography and determination of two new variants Hb (Chesapeake) and Hb-J (Bankok). J. Mol. Biol. 1991.
Colbert, E. H. (1955). Evolution of the Vertebrates Wiley, New York.
Dayhoff, M. O. (1972, 1973, 1976). Atlas of Protein Sequence and Structure, Vol. 5, Suppl. 1, and Suppl. 2, National Biochemical Research Foundation, Georgetown University Medical Center, Washington, D.C.
Dozy, A. M., Kleihaur, E. F., and Huisman, T. H. J. (1968). Heterogeneity of hemoglobins: Chromatography of various human and animal hemoglobin types on DEAE-Sephadex. J. Chromatog. 32723.
Garrick, L. M., Sharma, V. S., McDonald, M. J., and Ranney, H. M. (1975). Rat hemoglobin heterogeneity. Two structurally distinct α-chains and functional behavior of selected components. Biochem. J. 149245.
Garrick, M. D., and Huisman, T. H. J. (1968). Gene duplication of the α-chain of goat hemoglobin; evidence from a homozygous mutant. Biochim. Biophys. Acta 168585.
Harris, M. J., Wilson, J. B., and Huisman, T. H. J. (1972). Structural studies of hemoglobin α-chain from Virginia white tailed deer. Arch. Biochem. Biophys. 151540.
Huisman, T. H. J., and Schroeder, W. A. (1971). New Aspects of the Structure, Function and Synthesis of Hemoglobins National Biochemical Research Foundation, Butterworths, London.
Huisman, T. H. J., Brandt, G., and Wilson, J. B. (1968a). The structure of goat hemoglobins; structural studies of α-chains of the hemoglobins A and B. J. Biol. Chem. 2433675.
Huisman, T. H. J., Dozy, A. M., Wilson, J. B., Efremov, G. D., and Vaskov, B. (1968b). Sheep hemoglobin D, an α-chain variant with one apparent amino acid substitution. Biochim. Biophys. Acta 160467.
Jones, R. T., Brimhall, B., and Duerst, M. (1971). Amino acid sequence of the α- and β-chains of dog hemoglobin. Fed. Proc. Abs. 301259.
Kilmartin, J. V., and Clegg, J. B. (1967). Amino acid replacement in horse hemoglobin. Nature 213269.
Lalthantluanga, R., Gulati, J. M., and Barnabas, J. (1975). Hemoglobin genetics in bovines and equines. Ind. J. Biochem. Biophys. 1251.
McKenna, M. C. (1969). The origin and early differentiation of therian mammals. Ann. N.Y. Acad. Sci. 167217.
Moore, G. W., Barnabas, J., and Goodman, M. (1973). A method for constructing maximum parsimony ancestral amino acid sequences on a given network. J. Theor. Biol. 38459.
Morris, W. J. (1966). Fossil mammals from Baja California: New evidence on early Tertiary migrations. Science 1531376.
Moss, B., and Ingram, V. M. (1968). Hemoglobin synthesis during amphibian metamorphosis. J. Mol. Biol. 32481–492.
Ranjekar, P. K., and Barnabas, J. (1969). Hemoglobin phenotypes in water buffalo during development. Comp. Biochem. Physiol. 281395.
Romer, A. S. (1966). Vertebrate Paleontology University of Chicago Press, Chicago.
Schroeder, W. A., Shelton, J. R., Shelton, J. B., Robberson, B., and Babin, D. R. (1967). A comparison of amino acid sequences in the β-chain of adult bovine hemoglobins A and B. Arch. Biochem. Biophys. 120124.
Schroeder, W. A., Shelton, J. R., Shelton, J. B., Apell, G., Huisman, T. H. J., Smith, L. L., and Carr, W. R. (1972). Amino acid sequences in β-chains of adult bovine hemoglobin: C-Rhodesia and D-Zambia. Arch. Biochem. Biophys. 152222.
Wade, P. T., Skinner, A. F., Barnicot, N. A., and Huehn, E. R. (1969). Duplication of hemoglobin α-chain locus in Macaca irus. Protides Biol. Fluids Proc. Colloq. 17263.
Wilson, J. B., Edwards, W. C., McDaniel, M., Dobbs, M. M., and Huisman, T. H. J. (1966). Structure of sheep hemoglobins: The amino acid composition of the tryptic peptides of the non α-chains of hemoglobins A, B, C and F. Arch. Biochem. Biophys. 115385.
Wilson, J. B., Brandt, G., and Huisman, T. H. J. (1968). The structure of sheep hemoglobins: Structural studies of α-chains of the hemoglobins A and B. J. Biol. Chem. 2433687.
Wilson, J. B., Wrightstone, R. N., and Huisman, T. H. J. (1970). Hemoglobin α-chain duplication in barbary sheep (Ammotragus lervia). Nature 226354.
Wrightstone, R. N., Wilson, J. B., Miller, A., and Huisman, T. H. J. (1970). Structure of goat hemoglobins. IV. Third β-chain variant with three apparent amino acid substitutions. Arch. Biochem. Biophys. 138451.
Yamaguchi, Y., Horic, H., Matsuo, A., Shigeru, S., and Satake, K. (1965). Chemical structure of procine globin α. J. Biochem. (Tokyo) 58186.
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John, M.E., Barnabas, J. Gene diversity of bovid hemoglobins. Biochem Genet 16, 787–798 (1978). https://doi.org/10.1007/BF00484736
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DOI: https://doi.org/10.1007/BF00484736