Skip to main content
SpringerLink
Log in

Erythrocyte isozymes of phosphofructokinase in genetically high- and low-2,3-diphosphoglycerate rats

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

A major locus (Dpg) with two alleles (d and D) controls erythrocyte 2,3-diphosphoglycerate (DPG) levels in Long-Evans rats and is closely linked to a locus (Hbb) determining a hemoglobin electrophoretic polymorphism. Glycolytic intermediate levels and phosphofructokinase (PFK) kinetic studies suggest that in vivo PFK activity differences underlie the differences in DPG levels. We report here chromatographic and immunologic evidence that rat erythrocyte PFK is composed of two isozymes which elute from DEAE-Sephadex at positions identical to those of the isozymes in platelets and liver, respectively. The percentage of platelet-type PFK is significantly (P<0.05) smaller in low-DPG (dd) hemolysates than in DD hemolysates regardless of hemoglobin phenotype. When hemolysates were prepared in a stabilizing buffer, PFK specific activity was significantly (P<0.005) higher in DD rats. These data suggest that the PFK kinetic differences may result from alterations in the isozyme composition of active PFK.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Beutler, E. (1975). Red Cell Metabolism: A Manual of Biochemical Methods Grune and Stratton, New York.

    Google Scholar 

  • Brewer, G., Gilman, J., Noble, N., and Crews, V. (1978). Association in Long-Evans hooded rats of red cell 2,3-diphosphoglycerate levels with hemoglobin types. Biochem. Genet. 16695.

    Google Scholar 

  • Chassin, S., Kruckeberg, W., and Brewer, G. (1978). Thermal inactivation differences of phosphofructokinase in erythrocytes from genetically selected high and low DPG rat strains. Biochem. Biophys. Res. Commun. 831306.

    Google Scholar 

  • Dunaway, G. A., Jr., and Weber, G. (1974). Rat liver phosphofructokinase isozymes. Arch. Biochem. Biophys. 162620.

    Google Scholar 

  • Gilman, J. (1981). Red cell phosphofructokinase and pyruvate kinase activities correlate with genetic variation of 2,3-bisphosphoglycerate in rats. Biochem. Biophys. Res. Commun. 102766.

    Google Scholar 

  • Gonzalez, F., Tsai, M., and Kemp, R. (1975). Distribution of phosphofructokinase isozymes in rabbit, mouse, guinea pig and rat. Comp. Biochem. Physiol. 52B315.

    Google Scholar 

  • Kurata, N., Matsushima, T., and Sugimura, T. (1972). Multiple forms of phosphofructokinase in rat tissues and rat tumors. Biochem. Biophys. Res. Commun. 48473.

    Google Scholar 

  • Noble, N., and Brewer, G. (1972). Studies of the metabolic basis of the ATP-DPG differences in genetically selected high and low ATP-DPG rat strains. In Brewer, G. (ed.), Hemoglobin and Red Cell Structure and Function Plenum Press, New York, pp. 155–164.

    Google Scholar 

  • Noble, N., and Brewer, G. (1977). Identification of a major locus contributing to erythrocyte 2,3-diphosphoglycerate variability in hooded (Long-Evans) rats. Genetics 85669.

    Google Scholar 

  • Noble, N., and Tanaka, K. R. (1979). Erythrocyte enzymes in groups of Rattus Norvegicus with genetic differences in 2,3-diphosphoglycerate levels. Comp. Biochem. Physiol. 62B81.

    Google Scholar 

  • Noble, N., and Tanaka, K. R. (1981). Erythrocyte phosphofructokinase in rat strains with genetically determined differences in 2,3-diphosphoglycerate levels. Biochem. Genet. 1961.

    Google Scholar 

  • Reinhart, G., and Lardy, H. (1980). Rat liver phosphofructokinase: Kinetic activity under near-physiological conditions. Biochemistry 191477.

    Google Scholar 

  • Shapiro, A., Vinuela, E., and Maizel, J. (1967). Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28815.

    Google Scholar 

  • Tanaka, T., An, T., and Sakaue, Y. (1971). Studies on multimolecular forms of phosphofructokinase in rat tissues. J. Biochem. 69609.

    Google Scholar 

  • Vora, S. (1981). Isozymes of human phosphofructokinase in blood cells and cultured cell lines: Molecular and genetic evidence for a trigenic system. Blood 57724.

    Google Scholar 

  • Vora, S., Seaman, C., Durham, S., and Piomelli, S. (1980). Isozymes of human phosphofructokinase: Identification and subunit structural characterization of a new system. Proc. Natl. Acad. Sci. USA 7762.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Division of Hematology, Department of Medicine, Harbor-UCLA Medical Center, UCLA School of Medicine, 90509, Torrance, California

    N. A. Noble, L. H. Kuwashima, T. T. Togioka & K. R. Tanaka

Authors
  1. N. A. Noble
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. L. H. Kuwashima
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. T. T. Togioka
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. K. R. Tanaka
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

This investigation was supported in part by Grants 1 R01 HL 22672 and AM 14898 from the National Institutes of Health.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Noble, N.A., Kuwashima, L.H., Togioka, T.T. et al. Erythrocyte isozymes of phosphofructokinase in genetically high- and low-2,3-diphosphoglycerate rats. Biochem Genet 20, 1055–1065 (1982). https://doi.org/10.1007/BF00498932

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00498932

Key words

Search

Navigation