Purification and characterization of baboon endogenous virus DNA polymerase.
An RNA-directed DNA polymerase was purified from baboon endogenous type-C virus by successive column chromatography on DEAE cellulose, phosphocellulose and hydroxyapatite. The purified DNA polymerase has a molecular weight of 68 000, a pH optimum of 8.0, a Mn2+ optimum of 1 mM, and a KCl optimum of 40 mM. The purified enzyme transcribes heteropolymeric regions of viral 60--70 S RNA isolated from different type-C viruses. The purified enzyme is immunologically related to a similarly purified polymerase from the cat endogenous type-C virus RD114.
D000818:Animals; D000906:Antibodies; D000937:Antigen-Antibody Reactions; D002460:Cell Line; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification / Q000378:metabolism*; D000882:Haplorhini; D007700:Kinetics; D010215:Papio; D012190:Retroviridae / Q000201:enzymology*; D013698:Templates, Genetic
D000906:Antibodies; D004259:DNA-Directed DNA Polymerase