Bacteriophage T7 protein kinase is magnesium-dependent and sulfate-activated

Bacteriophage T7 protein kinase is magnesium-dependent and sulfate-activated

The cyclic-AMP-independent protein kinase induced by bacteriophage T7 in Escherichia coli was optimally activated by 60 mM magnesium. Substitution of magnesium sulfate for magnesium chloride produced approximately a two-fold increase in protein kinase activity, while magnesium acetate was least effe...

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Veröffentlicht in:Biochemical and biophysical research communications 1981-07, Vol.101 (1), p.201-207
Hauptverfasser: Rogers, Howell W., Phelps, Charles L.
Format: Artikel
Sprache:eng
Schlagworte:
Coliphages - enzymology
Enzyme Activation
Escherichia coli - enzymology
ionic strength
Kinetics
magnesium
Magnesium - pharmacology
Osmolar Concentration
phage T7
protein kinase
Protein Kinases - metabolism
Sulfates - pharmacology
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Zusammenfassung:The cyclic-AMP-independent protein kinase induced by bacteriophage T7 in Escherichia coli was optimally activated by 60 mM magnesium. Substitution of magnesium sulfate for magnesium chloride produced approximately a two-fold increase in protein kinase activity, while magnesium acetate was least effective in potentiating T7 protein kinase activity. Also, T7 protein kinase was demonstrated to be ionic strength dependent with maximal activity occurring at ionic strengths of 260 to 300 millimolar.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(81)80031-9