Chromatographic purification and characterization of EBV DNase from chemically induced lymphoid cells.
Epstein-Barr virus-associated deoxyribonuclease (EBV-DNase) was purified to homogeneity, as determined by silver staining, sequential column chromatography, and FPLC from Raji and P3HR-1 cells treated with 12-O-tetradecanoyl-phorbol-13-acetate and sodium butyrate. This viral protein was immunogenic and elicited high neutralization titer sera in rabbits. By silver staining of SDS-PAGE, Western immunoblot, and radioimmunoprecipitation using NPC patient sera and both polyclonal and monoclonal antibodies, the EBV DNase was identified as a 58K protein. The potential presence of two EBV DNases was also discussed.
Hwang
G Y
GY
Department of Biology, Utah State University, Logan 84322-5500.
Li
J K
JK
Chiou
J F
JF
Tan
R S
RS
D002087:Butyrates / Q000494:pharmacology*; D020148:Butyric Acid; D002460:Cell Line; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003851:Deoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004854:Herpesvirus 4, Human / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D008970:Molecular Weight; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D002087:Butyrates; D020148:Butyric Acid; D003851:Deoxyribonucleases; D013755:Tetradecanoylphorbol Acetate