Skip to main content
Log in

Glucose 6-phosphate dehydrogenase in rainbow trout

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Electrophoretic analysis of glucose 6-phosphate dehydrogenase from liver and blood of rainbow trout revealed a complex series of bands, which could differ between fish. The partial interconvertible nature of these bands was demonstrated with enzyme that had been incompletely inactivated at pH 8.4. In a single population of 40 fish, a homozygote and a heterozygote for an electrophoretic variant allele were found. We suggest that G6PD in rainbow trout liver and blood is determined by two alleles at a single locus, with posttranslational modification responsible for the complex electrophoretic patterns seen. The basis for this variation appears to be NADH binding to the protein molecule. Another variant and other properties of the enzyme are described.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Bonsignore, A., Lorenzoni, I., Cancedda, R., and De Flora, A. (1970). Distinctive patterns of NADP binding to dimeric and tetrameric glucose-6-phosphate dehydrogenase from human red cells. Biochem. Biophys. Res. Commun. 39142.

    Google Scholar 

  • Bonsignore, A., Cancedda, R., Nicolini, A., Damiani, G., and De Flora, A. (1971). Metabolism of human erythrocyte glucose-6-phosphate dehydrogenase. VI. Interconversation of multiple molecular forms. Arch. Biochem. Biophys. 147493.

    Google Scholar 

  • Cohen, P., and Rosemeyer, M. A. (1969). Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes. Eur. J. Biochem. 88.

    Google Scholar 

  • Fildes, R. A., and Parr, C. W. (1963). Human red-cell phosphogluconate dehydrogenases. Nature 200890.

    Google Scholar 

  • Hochachka, P. W. (1967). Metabolism during temperature compensation. In Prosser, C. L. (ed.), Molecular Mechanisms of Temperature Adaptation, Academic Press, New York, p. 177.

    Google Scholar 

  • Hochachka, P. W., and Somero, G. N. (1971). Biochemical adaptation to the environment. In Hoar, W. S., and Randall, D. J. (eds.), Fish Physiology, Vol. 6, Academic Press, New York, p. 99.

    Google Scholar 

  • Huehns, E. R., and Shooter, E. M. (1965). Human hemoglobins. J. Med. Genet. 248.

    Google Scholar 

  • IUPAC-IUB Commission on Biochemical Nomenclature (1971). The nomenclature of multiple forms of enzymes: Recommendations. J. Biol. Chem. 2466127.

    Google Scholar 

  • Jaenicke, R., and Knof, S. (1968). Molecular weight and quaternary structure of lactic dehydrogenase. 3. Comparative determination by sedimentation analysis, light scattering and osmosis. Eur. J. Biochem. 4157.

    Google Scholar 

  • Lyon, M. F. (1962). Sex chromatin and gene action in the mammalian X-chromosome. Am. J. Hum. Genet. 14135.

    Google Scholar 

  • Matsuda, T., and Yugari, Y. (1967). Glucose-6-phosphate dehydrogenase from rat liver. I. Crystallization and properties. J. Biochem. 61535.

    Google Scholar 

  • Niethammer, D., and Huennekens, F. M. (1971). Bound TPN as the determinant of polymorphism in methemoglobin reductase. Biochem. Biophys. Res. Commun. 45345.

    Google Scholar 

  • Ohno, S. (1967). Sex Chromosomes and Sex-Linked Genes, Springer-Verlag, New York.

    Google Scholar 

  • Ohno, S., Payne, A. W., Morrison, M., and Beutler, E. (1966). Hexose-6-phosphase dehydrogenase found in human liver. Science 1531015.

    Google Scholar 

  • Porter, I. H., Boyer, S. H., Watson-Williams, E. J., Adam, A., Szeinberg, A., and Siniscalco, M. (1964). Variation of glucose-6-phosphate dehydrogenase in different populations. Lancet 1895.

    Google Scholar 

  • Robinson, H. W., and Hogden, C. G. (1940). The biuret reaction in the determination of serum proteins. II. Measurements made by a Duboscq colorimeter compared with values obtained by the Kjeldahl procedure. J. Biol. Chem. 135727.

    Google Scholar 

  • Rudack, D., Chisholm, E. M., and Holten, D. (1971). Rat liver glucose-6-phosphate dehydrogenase. J. Biol. Chem. 2461249.

    Google Scholar 

  • Severson, A. R., Hubbard, D. D., and Gibson, D. M. (1973). Changes in distribution of lipid, glucose-6-phosphate dehydrogenase and malate enzyme within the liver lobule of the rat during adaptive hyperlipogenesis. Anat. Rec. 175231.

    Google Scholar 

  • Shatton, J. B., Halver, J. E., and Weinhouse, S. (1971). Glucose (hexose-6-phosphate) dehydrogenase in liver of rainbow trout. J. Biol. Chem. 2464878.

    Google Scholar 

  • Smithies, O. (1962). Molecular size and starch-gel electrophoresis. Arch. Biochem. Biophys. Suppl. 1125.

    Google Scholar 

  • Stegeman, J. J., and Goldberg, E. (1971). Distribution and characterization of hexose 6-phosphate dehydrogenase in trout. Biochem. Genet. 5579.

    Google Scholar 

  • Stegeman, J. J., and Goldberg, E. (1972). Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout. Comp. Biochem. Physiol. 43B41.

    Google Scholar 

  • Taketa, K., and Watanabe, A. (1971). Interconvertible microheterogeneity of glucose-6-phosphate dehydrogenase in rat liver. Biochim. Biophys. Acta 23519.

    Google Scholar 

  • Uyeno, T., and Miller, R. R. (1971). Multiple sex chromosomes in a Mexican cyprinodontoid fish. Nature 231452.

    Google Scholar 

  • Watanabe, A., and Taketa, K. (1973). Actinomycin D-insensitive induction of rat liver glucose-6-phosphate dehydrogenase by carbon tetrachloride injury. J. Biochem. 73771.

    Google Scholar 

  • Watanabe, A., Taketa, K., and Kosaka, K. (1972). Three interconvertible forms of glucose-6-phosphate dehydrogenase in human liver and erythrocyte. Enzyme 13203.

    Google Scholar 

  • Whitaker, J. R. (1963). Determination of molecular weights of proteins by gel filtration. Anal. Chem. 351950.

    Google Scholar 

  • WHO (1967). Standardization of Procedures for the Study of Glucose-6-phosphate Dehydrogenase, WHO Tech. Rep. Ser. No. 366.

  • Yamauchi, T., and Goldberg, E. (1973). Glucose 6-phosphate dehydrogenase from brook, lake, and splake trout: An isozymic and immunological study. Biochem. Genet. 10121.

    Google Scholar 

  • Yamauchi, T., Stegeman, J. J., and Goldberg, E. (1975). The effects of starvation and temperature acclimation on pentose phosphate pathway dehydrogenases in brook trout liver. Arch. Biochem. Biophys. 16713.

    Google Scholar 

  • Yoshida, A., and Watanabe, S. (1972). Human phosphoglycerate kinase. I. Crystallization and characterization of normal enzyme. J. Biol. Chem. 247440.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Supported in part by the State of California Department of Mental Hygiene and by USPHS Grants GM-15253, HD-04612, HD-00315, HD-05615, and HL-15125. One of us (S.D.C.) was a Special Postdoctoral Fellow of NIAMD (No. 1F03AM-40, 329-01) during part of this work.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Cederbaum, S.D., Yoshida, A. Glucose 6-phosphate dehydrogenase in rainbow trout. Biochem Genet 14, 245–258 (1976). https://doi.org/10.1007/BF00484764

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484764

Key words

Navigation