Purification of a protein kinase and two phosphate acceptor proteins from vaccinia virions.
A novel protein kinase that requires protamine as an activator to catalyze the phosphorylation of viral acceptor proteins was extracted from vaccinia virus cores with deoxycholate and purified 250-fold by DNA-cellulose and DEAE-cellulose column chromatography. The enzyme has a molecular weight of 62,000 as determined by sucrose gradient sedimentation. Two heat-stable phosphate acceptor proteins were extracted from virus particles with a nonionic detergent and purified by heat treatment, precipitation with organic solvents, and CM-cellulose chromatography. The molecular weights of the phosphate acceptor proteins, determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis, are 38,500 and 11,700.
D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008970:Molecular Weight; D011479:Protamines; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D014616:Vaccinia virus / Q000032:analysis* / Q000201:enzymology; D014764:Viral Proteins / Q000302:isolation & purification*
D011479:Protamines; D014764:Viral Proteins; D011494:Protein Kinases