Isolation and characterization of a homogeneous DNA-protein complex from adenovirus type 2 virion.
Adenovirus DNA-protein complex purified by sedimentation on a sucrose gradient containing 4 M-guanidine hydrochloride was found to contain other virion proteins in addition to the terminal protein of mol. wt. 55000. In this report, we describe a simple and rapid method for the isolation of a homogeneous DNA-protein complex. The procedure involves gel electrophoresis of the complex on agarose in the presence of sodium dodecyl sulphate. DNA was found to migrate into the gel with a single protein of mol. wt. 55000 tightly attached to it. Restriction enzyme cleavage analysis of the DNA-protein complex shows that the protein is associated with the two terminal fragments.
D000260:Adenoviruses, Human / Q000032:analysis* / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D004279:DNA, Viral / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D011485:Protein Binding; D014764:Viral Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D004279:DNA, Viral; D014764:Viral Proteins