Purification of Epstein-Barr virus associated DNase with affinity chromatography of nasopharyngeal carcinoma patient serum.
Epstein-Barr virus associated DNase in the homogeneous form can be purified by chromatographys using CH-sepharose 4B column conjugated with nasopharyngeal carcinoma patient serum, DNA cellulose and phosphocellulose in that sequence. The molecular weight of this enzyme is shown to be 51 kilo-daltons in silver-staining and immunostains. Among various methods for keeping DNase activity, the addition of BSA and dialysis in glycerol or ethylene glycol immediately after the enzyme purification is suggested.
Chiou
J F
JF
Department of Bacteriology, College of Medicine, National Taiwan University, Taipei, ROC.
Cheng
Y C
YC
Hsu
M M
MM
D002087:Butyrates / Q000494:pharmacology; D020148:Butyric Acid; D002277:Carcinoma / Q000201:enzymology / Q000382:microbiology*; D002846:Chromatography, Affinity; D003851:Deoxyribonucleases / Q000096:biosynthesis / Q000276:immunology / Q000302:isolation & purification*; D004795:Enzyme Stability; D004854:Herpesvirus 4, Human / Q000201:enzymology*; D006801:Humans; D009303:Nasopharyngeal Neoplasms / Q000201:enzymology / Q000382:microbiology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D002087:Butyrates; D020148:Butyric Acid; D003851:Deoxyribonucleases; D013755:Tetradecanoylphorbol Acetate