Identification of an ionic strength sensitive nuclear protein kinase activity from the cervical carcinoma HeLa.
A cyclic nucleotide independent, serine-threonine protein kinase activity has been purified approximately 700 fold from the nuclei of HeLa cells. This activity has a very strict ionic strength requirement. Maximum activity is obtained in a monovalent cation environment under 50 mM, where Mg++ is preferred over Mn++ as the required divalent cation.
D002467:Cell Nucleus / Q000201:enzymology*; D002712:Chlorides; D006367:HeLa Cells / Q000201:enzymology*; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D015636:Magnesium Chloride; D008345:Manganese / Q000494:pharmacology; D017895:Manganese Compounds; D009994:Osmolar Concentration; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification*
D002712:Chlorides; D017895:Manganese Compounds; D015636:Magnesium Chloride; D008345:Manganese; D011494:Protein Kinases; D008274:Magnesium; C025340:manganese chloride