Abstract
A method is described for detecting the electrophoretic pattern of the enzyme 2,3-diphosphoglycerate mutase (2,3-DPGM) after starch gel electrophoresis. In addition, a genetic variant found in a Canadian Eskimo family is described. The pattern of this (presumably) heterozygous phenotype is consistent with a dimeric structure of the enzyme.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Benesch, R., and Benesch, R. E. (1967). The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. Biophys. Res. Commun. 26 162.
Benesch, R., and Benesch, R. E. (1969). Intracellular organic phosphates as regulators of oxygen release by haemoglobin. Nature 221 618.
Bunn, H. F., and Jandl, J. H. (1970). Control of hemoglobin function within the red cell. New Engl. J. Med. 282 1414.
Chanutin, A., and Curnish, R. R. (1967). Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes. Arch. Biochem. 121 96.
Chen, S.-H., and Giblett, E. R. (1971). Genetic variation of soluble glutamic-oxaloacetic transaminase in man. Am. J. Human Genet. 23 (in press).
Eaton, J. W., Brewer, G. J., and Grover, R. F. (1969). Role of red cell 2,3-diphosphoglycerate in the adaptation of man to altitude. J. Lab. Clin. Med. 73 603.
Harris, H., Hopkinson, D. A., Luffman, J. E., and Rapley, S. (1968). Electrophoretic variation in erythrocyte enzymes. In Beutler, E. (ed.), Hereditary Disorders of Erythrocyte Metabolism, Grune and Stratton, New York, pp. 1–20.
Joyce, B. K., and Grisolia, S. (1959). The purification and properties of muscle diphosphoglycerate mutase. J. Biol. Chem. 234 1330.
Lenfant, C., Torrance, J., English, E., Finch, C. A., Reynafarje, C., Ramos, J., and Faura, J. (1968). Effect of altitude on oxygen binding by hemoglobin and on organic phosphate levels. J. Clin. Invest. 47 2652.
Rapoport, S., and Luebering, J. (1950). The formation of 2,3-diphosphoglycerate in rabbit erythrocytes: The existence of a diphosphoglycerate mutase. J. Biol. Chem. 183 507.
Rapoport, S., and Luebering, J. (1952). An optical study of diphosphoglycerate mutase. J. Biol. Chem. 196 583.
Rose, Z. B. (1968). The purification and properties of diphosphoglycerate mutase from human erythrocytes. J. Biol. Chem. 243 4810.
Rose, Z. B. (1970). Enzymes controlling 2,3-diphosphoglycerate in human erythrocytes. Federation Proc. 29 1105.
Schröter, W. (1965). Kongenitale Nichtsphärocytäre hämolytische Anämie bei 2,3-Diphosphoglyceratmutase-Mangel der Erythrocyten im frühen Säuglingsalter. Klin. Wochschr. 43 1147.
Author information
Authors and Affiliations
Additional information
This work was supported by PHS grant AM 09745.
Rights and permissions
About this article
Cite this article
Chen, SH., Anderson, J.E. & Giblett, E.R. 2,3-diphosphoglycerate mutase: Its demonstration by electrophoresis and the detection of a genetic variant. Biochem Genet 5, 481–486 (1971). https://doi.org/10.1007/BF00487137
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00487137