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The extent of direct stimulation by spermine of reactions catalysed by nuclear N1 and N2 protein kinases purified from liver and prostate depends critically on the nature of the protein substrate. The chemically inert Co(NH3)36+ ion exerts effects on protein kinase reactions similar to those of spermidine or spermine. This enhancement of the phosphorylation of various protein substrates by polyamines or Co(NH3)63+ by purified nuclear protein kinase preparations was studied in relation to effects of temperature, pH and other factors. The results provide further support for our hypothesis [Ahmed, Wilson, Goueli & Williams-Ashman (1978) Biochem. J. 176, 739-750] that the enhancement of certain protein kinase reactions by polycations relates primarily to their interaction with the protein substrate, yielding more favourable conformations for phosphorylation by the protein kinase, rather than a direct effect on its catalytic activity.
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
June 1979,
The Journal of biological chemistry,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
September 1973,
Biochemical and biophysical research communications,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
December 1986,
The Biochemical journal,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
February 1985,
Biochimica et biophysica acta,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
April 1971,
Proceedings of the National Academy of Sciences of the United States of America,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
October 1985,
The Journal of biological chemistry,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
June 1980,
Biochemical and biophysical research communications,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
August 1982,
FEBS letters,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
March 1979,
The Kobe journal of medical sciences,
K Ahmed, and
S A Goueli, and
H G Williams-Ashman
July 1985,
Biochimica et biophysica acta,
