Electron Microscopy of Muscle Phosphorylases b and a

  • N. A. Kiselev
  • F. Ya. Lerner
  • N. B. Livanova
Conference paper

Abstract

Muscle glycogen phosphorylase exists in two enzymatically inter- convertible forms: phosphorylase a and phosphorylase b. It has been shown that phosphorylase a in solution is a tetramer of molecular weight 400000 (s=13,2S), and phosphorylase b is a dimer of molecular weight 200000 (1). In the presence of p-chlormercuribenzoate (2) phosphorylases a and b dissociate into four and two monomers, respectively, both having the same molecular weight. On conversion of phosphorylase b into a, in the presence of ATP, Mg2+ and phosphorylase b kinase, one phosphate group appears to be bonded to the serine residue per monomer of the enzyme (3). If phosphorylase a is fully active in the native state without 5′-AMP, phosphorylase b, the non-phosphorylated form of the enzyme, is active only in the presence of 5′AMP or IMP with protamin (4,5). The ultracentrifuge studies have shown that the dimeric form of phosphorylase b is converted into the tetrameric form (s=13,2S) in the presence of a mixture of 0,001M-AMP+0,03M cysteine+0,01M Mg2+ (6) or 0,001M 5′-IMP+ 0,0001M protamin or protamin only (7).

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References

  1. 1.
    Cohen Ph., Duewer Th., Fischer E.H. Biochemistry, 10, 2683 (1971).CrossRefGoogle Scholar
  2. 2.
    Madsen N.B. & Cori C.F. J.Biol.Chem., 223, 1055 (1956).Google Scholar
  3. 3.
    Nolan C., Novoa W.B. & Fischer E.H. Biochemistry, 542 (1964).Google Scholar
  4. 4.
    Cori G.T., Colowick S.P. & Cori C.F. J.Biol.Chem., 123, 381 (1938)Google Scholar
  5. 5.
    Krebs E.G. Biochim Biophys. Acta, 15. 508 (1954).CrossRefGoogle Scholar
  6. 6.
    Fischer E.H. & Krebs E.G. J. Biol. Chem., 231, 65 (1958).Google Scholar
  7. 7.
    Silonova G.V., Lissovskaya N.P. & Pikhelgas V. Ya. Doklady Akademii Nauk SSSR, 169, 483 (1966)Google Scholar
  8. 8.
    Madsen N.B. & Cori C.F. Biochim. et Biophys.Acta, 15,516 (1954).CrossRefGoogle Scholar
  9. 9.
    Lissovskaya N.P., Livanova N.B. & Silonova G.V. Biochimiya, 22, 1012 (1964).Google Scholar
  10. 10.
    Krebs E.G., Kent A.B. & Fischer E.H. J.Biol.Chem., 231,73 (1958)Google Scholar
  11. 11.
    Kosourov G.I., Livshits I.E. & Kiselev N.A. Kristallografiya, 16, 813 (1971).Google Scholar
  12. 12.
    Kiselev N.A., Lerner F. Ya. & Livanova N.B. Molekulyarnaya Biologiya, 5.642 (1971) (Mol.Biol. in Russian).Google Scholar
  13. 13.
    Klug A. & De Rosier D.J. Nature. 212, 29 (1966).CrossRefGoogle Scholar
  14. 14.
    Watson I.D. Biochira. et Biophys. Acta, 13, 10 (1954).CrossRefGoogle Scholar
  15. 15.
    Vainshtein B.K. Diffraction of X-Rays by Chain Molecules, Amsterdam: Elsevier. 1966.Google Scholar
  16. 16.
    Mikhailov A.M. Kristallografiya, 15. 818 (1970).Google Scholar
  17. 17.
    Pranklin R.E. & Klug A. Biochim. et Biophys.Acta, 19,403 (1956).CrossRefGoogle Scholar
  18. 18.
    Chignell D.A., Gratzer W.B. & Valentine R.C. Biochemistry, 2, 1082 (1968).CrossRefGoogle Scholar
  19. 19.
    Klug A. In “Symmetry and Function of Biol. System at the Macromolecular Level”. Ed.: A.Engström a. B.Strandberg Almqvist & Wiksell, Stockholm. 1970.Google Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1972

Authors and Affiliations

  • N. A. Kiselev
    • 1
  • F. Ya. Lerner
    • 1
  • N. B. Livanova
    • 2
  1. 1.Institute of Crystallography of the Academy of Sciences of the USSRMoscowUSSR
  2. 2.Bach Institute of Biochemistry of the Academy of Sciences of the USSRMoscowUSSR

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