Purification of Epstein-Barr virus DNA polymerase from P3HR-1 cells. |
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| Authors: | B Kallin, L Stern s, A K Saemundssen, J Luka, H J rnvall, B Eriksson, P Z Tao, M T Nilsson, G Klein |
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| Affiliation: | B Kallin, L Sternås, A K Saemundssen, J Luka, H Jörnvall, B Eriksson, P Z Tao, M T Nilsson, and G Klein |
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| Abstract: | The Epstein-Barr virus DNA polymerase was purified from extracts of P3HR-1 cells treated with n-butyrate for induction of the viral cycle. Sequential chromatography on DNA cellulose, phosphocellulose, and blue Sepharose yielded an enzyme preparation purified more than 1,300-fold. The purified enzyme was distinct from cellular enzymes but resembled the viral DNA polymerase in cells infected with herpes simplex virus type 1 or 2. The active enzyme had an apparent molecular weight of 185,000 as estimated by gel filtration on Sephacryl S-300. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a major polypeptide corresponding to a molecular weight of ca. 110,000. This polypeptide correlated with the catalytic function of the purified enzyme, whereas the other, less abundant polypeptides did not. By immunoblotting, the 110,000-molecular-weight polypeptide could be identified as a viral polypeptide. It could not be determined whether the native enzyme was composed of more than one polypeptide. |
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