Isolation and Characterization of a Homogeneous DNA-Protein Complex from Adenovirus Type 2 Virion
- 1 November 1979
- journal article
- research article
- Published by Microbiology Society in Journal of General Virology
- Vol. 45 (2) , 519-525
- https://doi.org/10.1099/0022-1317-45-2-519
Abstract
Adenovirus DNA-protein complex purified by sedimentation on a sucrose gradient containing 4 M-guanidine hydrochloride contained other virion proteins in addition to the terminal protein of MW 55,000. A simple and rapid method for the isolation of a homogeneous DNA-protein complex is described. The procedure involves gel electrophoresis of the complex on agarose in the presence of sodium dodecyl sulfate. DNA migrated into the gel with a single protein of MW 55,000 tightly attached to it. Restriction enzyme cleavage analysis of the DNA-protein complex shows that the protein is associated with the 2 terminal fragments.This publication has 4 references indexed in Scilit:
- Adenovirus type 2 terminal protein: purification and comparison of tryptic peptides with known adenovirus-coded proteinsJournal of Virology, 1979
- Physical organization of subgroup B human adenovirus genomesJournal of Virology, 1977
- Mouse adenovirus: Growth of plaque-purified FL virus in cell lines and characterization of viral DNAVirology, 1977
- Specific interaction of a protein(s) at or near the termini of adenovirus 2 DNABiochemical and Biophysical Research Communications, 1977