Protein kinase activity associated with the surface of guinea pig macrophages.
Protein kinase activity has been detected associated with the outer surface of guinea pig peritoneal macrophages. Macrophages incubated with [gamma-32P]ATP incorporated 32P-phosphate into cell-associated proteins. Inorganic phosphate did not compete, nor could inorganic [32P]phosphate substitute as the phosphate donor, demonstrating that transfer of phosphate from ATP to protein is direct and extracellular. The macrophage-associated protein kinase was also shown to phosphorylate added acceptor protein (histone) and to be tightly associated with the cell surface. Thus, a new ectoenzyme, a protein kinase, has been detected in macrophages.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D006168:Guinea Pigs; D008264:Macrophages / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
D000255:Adenosine Triphosphate; D011494:Protein Kinases