A protein kinase activity from rat cerebellum stimulated by guanosine-3′:5′-monophosphate

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Abstract

The influence of cyclic nucleotides on a protein kinase activity present in the 50,000 × g supernatant of rat cerebellum has been studied. cGMP (3 × 10−7M) increased histone phosphorylation by about 90 %. The apparent Ka for cGMP was 3.6 × 10−8M. cAMP had a similar effect, but higher concentrations (10−5M) were required to obtain a comparable stimulation, the apparent Ka being 9 × 10−7M. In a phosphate free buffer cGMP had only a slight effect on the rate of phosphorylation, whereas cAMP stimulated the reaction by 100%. The addition of phosphate resulted in a twofold increase of the reaction stimulated by cGMP and in a marked decrease of the phosphorylation stimulated by cAMP. In addition, different pH optima for the two reactions were observed. It is concluded that in the rat cerebellum a cGMP stimulated protein kinase exists.

References (16)

  • J.A. Ferrendelli et al.

    Biochem. Biophys. Res. Comm

    (1972)
  • J.F. Kuo et al.

    J. Biol. Chem

    (1972)
  • J.F. Kuo et al.

    J. Biol. Chem

    (1970)
  • A. Läuchli

    Int. J. Appl. Rad. Isotopes

    (1969)
  • O.H. Lowry et al.

    J. Biol. Chem

    (1951)
  • H. Maeno et al.

    J. Biol. Chem

    (1972)
  • J.F. Kuo et al.

    J. Biol. Chem

    (1971)
  • D.A. Walsh et al.

    J. Biol. Chem

    (1968)
There are more references available in the full text version of this article.

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Presented in part at the Fifth International Congress on Pharmacology July 23–28, 1972, San Francisco, California.

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