Abstract
We have compared the solubility, kinetic, immunological, and electrophoretic properties of erythrocyte pyruvate kinase from normal dogs and Basenji dogs with congenital hemolytic anemia due to pyruvate kinase deficiency. Differences can be detected between the two enzymes by all methods. The enzyme from the affected animals has a greater solubility in ammonium sulfate. It has a lower K m for phosphoenolpyruvate, while the K m for ADP is increased. This enzyme is not inhibited by ATP or activated by fructose 1,6-diphosphate. The enzyme from the affected animals has none of the allosteric properties characteristic of the normal canine enzyme. No difference can be detected by enzyme inactivation with rabbit antiserum against the human erythrocyte enzyme, but a slight spur is observed on comparison of the two enzymes by Ouchterlony immunodiffusion. The enzymes also differ in their electrophoretic mobilities on starch gel electrophoresis.
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References
Beutler, E. (1969). Genetic disorders in red cell metabolism. Med. Clin. North Am. 53813.
Black, J. A., Chern, C. J., and Rittenberg, M. B. (1975). Canine erythrocyte pyruvate kinase. I. Properties of the normal enzyme. Biochem. Genet. 13331.
Bucher, T., and Pfleiderer, G. (1955). Pyruvate kinase from muscle. Meth. Enzymol. 1435.
Busch, D., and Pelz, K. (1966). Erythrocytenisolierung aus Blut mit Baumwolle. Klin. Wschr. 16983.
Campos, J. O., Koler, R. D., and Bigley, R. H. (1965). Kinetic differences between human red cell and leucocyte pyruvate kinase. Nature 208194.
Davidsohn, I., and Henry, J. B. (eds.) (1969). Todd-Sanford Clinical Diagnosis by Laboratory Methods, 14th ed., Saunders, Philadelphia, p. 155.
Dhindsa, D. S., Black, J. A., Koler, R. D., Templeton, J. W., and Metcalfe, J. (1974). Respiratory characteristics of Basenji dog blood with erythrocyte pyruvate kinase abnormality. Fed. Proc. 33456.
Hill, A. V. (1910). The possible effects of the aggregation of the molecules of hemoglobin on its dissociation curves. J. Physiol. (Lond.) 404.
Koler, R. D., Bigley, R. H., Jones, R. T., Rigas, D. A., Vanbellinghen, P., and Thompson, P. (1964). Pyruvate kinase: Molecular differences between human red cell and leukocyte enzyme. Cold Spring Harbor Symp. Quant. Biol. 29213.
Paglia, D. E., and Valentine, W. N. (1970). Evidence for molecular alteration of pyruvate kinase as a consequence of erythrocyte aging. J. Lab. Clin. Med. 76202.
Perutz, M. F., and Lehmann, H. (1968). Molecular pathology of human hemoglobin. Nature 219902.
Rose, I. A., and Warms, J. V. B. (1966). Control of glycolysis in the human red blood cell. J. Biol. Chem. 2414848.
Searcy, G. P., Miller, D. R., and Tasker, J. B. (1971). Congenital hemolytic anemia in the Basenji dog due to erythrocyte pyruvate kinase deficiency. Can. J. Comp. Med. 3567.
Staal, G. E. J., Koster, J. F., and Nijessen, J. G. (1972). A new variant of red cell pyruvate kinase deficiency. Biochim. Biophys. Acta 258685.
Standerfer, R. J., Templeton, J. W., and Black, J. A. (1974). Anomalous pyruvate kinase deficiency in the Basenji dog. Am. J. Vet. Res. 351541.
Tasker, J. B., Severin, G. A., Young, S., and Gillette, E. L. (1969). Familial anemia in the Basenji dog. J. Am. Vet. Assoc. 154158.
Torrance, J., Jacobs, P., Restrepo, A., Eschbach, J., Lenfant, C., and Finch, C. A. (1970). Intraerythrocytic adaptation to anemia. New Engl. J. Med. 283165.
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This work was supported by U.S.P.H. Grant AM-13173 and the Medical Research Foundation of Oregon. R.J.S. was the recipient of an Oregon Heart Association Summer Fellowship.
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Standerfer, R.J., Rittenberg, M.B., Chern, C.J. et al. Canine erythrocyte pyruvate kinase. II. Properties of the abnormal enzyme associated with hemolytic anemia in the basenji dog. Biochem Genet 13, 341–351 (1975). https://doi.org/10.1007/BF00485819
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DOI: https://doi.org/10.1007/BF00485819