Phosphorylation of a Dogfish Skeletal Muscle Protein Related to Parvalbumin

  • H. E. Blum
  • S. Pocinwong
  • E. H. Fischer
Conference paper

Abstract

A class of proteins was isolated from the skeletal muscle of the Pacific dogfish (Squalus sucklii) with properties extremely similar to those of the parvalbumins in that they display the same characteristic UV-spectrum, strong affinity for calcium and immunological cross-reactivity with antibodies prepared against dogfish parvalbumin. Though they are found in three polymeric states with MW of ca. 350,000, 75,000, and 25,000, they dissociate in sodium dodecylsulfate into subunits of MW ca. 12,000 identical in size to the parvalbumins. The three high molecular weight species are readily phosphorylated by a cyclic nucleotide-independent dogfish protein kinase, but not by phosphorylase kinase. One phosphate is introduced per subunit which can be released by a dogfish protein phosphatase different from phosphorylase phosphatase. By contrast, no phosphorylation of parvalbumins could be demonstrated under any circumstances. These data might suggest that the phosphate-acceptor protein represents a physiologically active form of the parvalbumins.

Keywords

Arthritis EDTA Turkey Tryptophan Naphthalene 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Benzonana, G., Capony, J.-P, and Pechare, J.-F. (1972), Biochim. Biophys. Acta 278, 110.Google Scholar
  2. Briggs, F. N., and Fleishman, G. (1965), J. Gen. Physiol. 49, 131.CrossRefGoogle Scholar
  3. Capony, J.-P., Ryden, L., Demaille, J., and Pechare, J.-F. (1973), Eur. J. Biochem. 32, 97.CrossRefGoogle Scholar
  4. Clausen, J. in “Laboratory Techniques in Biochemistry and Molecular Biology” (T. S. Work and E. Work, eds.), North-Holland Publishing Company, Amsterdam, London, 1972, 530–1.Google Scholar
  5. Coffee, C. J., and Bradshaw, R. A. (1973), J. Biol. Chem. 248, 3305.Google Scholar
  6. Connell, J. J. (1953), Biochem. J. 55, 378.Google Scholar
  7. Deuticke, H. J. (1934), Z. Physiol. Chem. 224, 216.CrossRefGoogle Scholar
  8. England, P. J., Stull, J. T., and Krebs, E. G. (1972), J. Biol. Chem. 247, 5275.Google Scholar
  9. England, P. J., Stull, J. T., Huang, T. S., and Krebs, E. G. (1973), Third Intl. Symposium on Metabolic Interconversion of Enzymes, Seattle, Washington, USA, June 5–8.Google Scholar
  10. Focant, B., and Pechére, J.-F. (1965), Arch. Intern. Physiol. Biochem. 73, 334.CrossRefGoogle Scholar
  11. Greaser, M. L., Yamaguchi, M., Brekke, C., Potter, J., and Gergely, J. (1973), Cold Spring Harbor Symp. Quant. Biol. 37, 235.CrossRefGoogle Scholar
  12. Greaser, M. L., and Gergely, J. (1973), J. Biol. Chem. 248, 2125.Google Scholar
  13. Heizmann, C., Malencik, D., and Fischer, E. H. (1973), in preparation.Google Scholar
  14. Hendrickson, W. A., and Karle, J. (1973), J. BioZ. Chem. 248, 3327.Google Scholar
  15. Henrotte, J. G. (1960), Biochim. Biophys. Acta 39, 103.CrossRefGoogle Scholar
  16. Jebsen, J. W. and Hamoir, G. (1958), Acta Chem. Scand.12, 1851.Google Scholar
  17. Kretsinger, R. H., and Nockolds, C. E. (1973), J. Biol. Chem. 248, 3313.Google Scholar
  18. Lehman, W., Kendrick-Jones, J., and Szent-Györgyi, A. G. (1973), Cold Spring Harbor Symp. Quant. Biol. 37, 319.CrossRefGoogle Scholar
  19. Lowe, M., Blum, H. E., Pocinwong, S., Fischer, E. H., and Benditt, E. (1973), in preparation.Google Scholar
  20. Lowey, S., and Holt, J. C. (1973), Cold Spring Harbor Symp. Quant. Biol. 37, 19.CrossRefGoogle Scholar
  21. Lowry, 0. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951), J. Biol. Chem. 193, 265.Google Scholar
  22. Pechére, J.-F., and Focant, B. (1965), Biochem. J. 96, 113.Google Scholar
  23. Pechére, J.-F., (1968), Comp. Biochem. Physiol. 24, 289.Google Scholar
  24. Pechére, J.-F., Capony, J.-P., Ryden, L., and Demaille, J. (1971a), Biochem. Biophys. Res. Comm. 43, 1106.CrossRefGoogle Scholar
  25. Pechere, J.-F., Demaille, J., and Capony, J.-P. (1971b), Biochim. Biophys. Acta 236, 391.Google Scholar
  26. Perrie, W. T., Smillie, L. B., and Perry, S. V. (1972), Biochem. J. 128, 105 P.Google Scholar
  27. Perrie, W. T., Smillie, L. B., and Perry, S. V. (1973), Cold Spring Harbor Symp. Quant. Biol. 37, 17.CrossRefGoogle Scholar
  28. Perry, S. V., and Cole, H. A. (1973), Biochem. J. 131, 425.Google Scholar
  29. Pratje, E., and Heilmeyer, L. M. G. (1972), FEBS Lett. 27, 89.CrossRefGoogle Scholar
  30. Pratje, E., and Heilmeyer, L. M. G. (1973), Third Intl. Symposium on Metabolic Interconversion of Enzymes, Seattle, Washington, USA, June 5–8.Google Scholar
  31. Heimann, E. M., Walsh, D. A., and Krebs, E. G. (1971), J. Biol. Chem. 246, 1986.Google Scholar
  32. Shiina, S., and Mizuhira, V. (1971), Jap. Heart J. 12, 90.CrossRefGoogle Scholar
  33. Stull, J. T., Brostrom, C. 0., and Krebs, E. G. (1972), J. Biol. Chem. 247, 5272.Google Scholar
  34. Stull, J. T., England, P. J., Brostrom, C. 0., and Krebs, E. G. (1973), Cold Spring Harbor Symp. Quant. Biol. 37, 263.CrossRefGoogle Scholar
  35. Turner, D. C., Wallimann, T., and Eppenberger, H. M. (1973), Proc. Nat. Acad. Sci. USA 70, 702.CrossRefGoogle Scholar
  36. Walsh, D. A., Ashby, C. D., Gonzalez, C., Calkins, C., Fischer, E. H., and Krebs, E. G. (1971), J. Biol. Chem. 247, 1977.Google Scholar
  37. Weber, K., and Osborn, M. (1969), J. Biol. Chem. 244, 4406.Google Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1974

Authors and Affiliations

  • H. E. Blum
    • 1
  • S. Pocinwong
    • 1
  • E. H. Fischer
    • 1
  1. 1.Department of BiochemistryUniversity of WashingtonSeattleUSA

Personalised recommendations