Plasma membrane protein kinase activity in normal and Rous sarcoma virus-transformed chick embryo fibroblasts.
A preliminary study has been carried out to investigate the effect of Rous sarcoma virus transformation on plasma membrane protein kinase activity in chick embryo fibroblasts. Enzyme activity was measured using an in vitro phosphorylation method employing [gamma-32P]ATP with isolated plasma membranes serving as the source of both protein kinase and protein substrate. In general, the enzymatic properties observed were similar to those of other known protein kinases. However, for maximal activity a marked dependence on high Mg2+ concentrations was noted. Evidence was obtained which showed that cyclic nucleotide-dependent protein kinases were present in membranes from normal cells, but none could be measured in preparations from transformed cells. In addition, transformation appeared to result in a slight increase in basal plasma membrane protein kinase activity.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001358:Avian Sarcoma Viruses; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D002472:Cell Transformation, Viral; D002642:Chick Embryo; D005347:Fibroblasts / Q000201:enzymology; D008565:Membrane Proteins / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology; D009712:Nucleotides, Cyclic / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*
D008565:Membrane Proteins; D009712:Nucleotides, Cyclic; D000255:Adenosine Triphosphate; D011494:Protein Kinases