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The occurrence of multiple protein kinases, distinguished with respect to molecular weight and preference for acceptor proteins, was demonstrated in Ascaridia galli. The molecular weights of the cyclic AMP-dependent protein kinase and of phosvitin kinase I and II - both independent of cyclic AMP-were determined to be 160000, greater than 200000 and 40000, respectively. The cyclic AMP-dependent protein kinase preferred histones and kemptide as acceptor substrates; stimulation of enzyme activity was up to 4-fold by cyclic AMP. The activities of phosvitin kinase I and II were found to be effectively inhibited by suramin. The inhibition constants were calculated to be 2 microM and 5 microM, respectively. In addition, stibophen turned out to be a potent inhibitor of phosvitin kinase I; the inhibition constant was determined to be 10 microM.
E Ossikovski, and
R D Walter
June 1980,
Archives of biochemistry and biophysics,
E Ossikovski, and
R D Walter
January 1983,
Annales d'endocrinologie,
E Ossikovski, and
R D Walter
May 1978,
National Cancer Institute monograph,
E Ossikovski, and
R D Walter
January 1974,
Methods in enzymology,
E Ossikovski, and
R D Walter
April 1979,
Biochimica et biophysica acta,
E Ossikovski, and
R D Walter
January 1980,
Annual review of pharmacology and toxicology,
E Ossikovski, and
R D Walter
January 1981,
Current topics in cellular regulation,
E Ossikovski, and
R D Walter
January 1975,
Biochimie,
E Ossikovski, and
R D Walter
January 1975,
Naunyn-Schmiedeberg's archives of pharmacology,
E Ossikovski, and
R D Walter
August 1976,
Biochemical and biophysical research communications,
