Abstract
Adenovirus type 12 (Ad12) tumor (T) antigen, extracted from Ad12-transformed hamster cells and partially purified (>500-fold) by chromatography on double-stranded DNA-cellulose, contains DNA polymerase α activity which is partially inhibited by antibodies reacting with T antigen. The DNA polymerase and T antigen can be completely separated by chromatography on single-stranded DNA-cellulose to which T antigen does not bind. Antibodies reacting with T antigen have no inhibitory effect on the isolated DNA polymerase. The fraction eluting in the void volume of a single-stranded DNA-cellulose column containing >1200-fold purified T antigen stimulates markedly the activity of DNA polymerase α with “native” DNA template; with the “activated” DNA template the stimulation is less prominent. This stimulation is not significantly affected by T antigen-reactive antibodies. An analogous fraction of control BHK21 cells has similar stimulatory effects on the isolated DNA polymerase α, indicating that the stimulatory activity is probably not attributable to T antigen. The T-antigen polypeptides were immunoprecipitated from >1200-fold-purified preparations by antibodies from tumor-bearing hamsters and were identified as a major peptide of molecular weight 50,000 and a minor species of molecular weight 11,000.
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