Purification and some properties of an extracellular ribonuclease with antiviral activity against tobacco mosaic virus from Bacillus cereus.
A new ribonuclease (RNase) with tobacco mosaic virus inhibition was isolated and purified from Bacillus cereus ZH14 through ammonium sulfate precipitation, ultrafiltration, ion-exchange chromatography of DEAE-Sephadex A-50 column, and gel chromatography of Sephacryl S-200HR column. The enzyme was purified approximately 134-fold with a recovery of 9.2%. The RNase had an MW of 75.6 kDa in SDS-PAGE, which differed from RNases reported previously. The inhibitory activity of the RNase in the purification process against tobacco mosaic virus was tested, and the percentage inhibition of the purified RNase (48 U/ml) reached 90%. The protein could tolerate 90 degrees C and pH 4.0.
Zhou
Wen-Wen
WW
College of Food Science and Nutritional Engineering, China Agricultural University, 100083 Beijing, China. zww2003@gmail.com
Niu
Tian-Gui
TG
D000998:Antiviral Agents / Q000302:isolation & purification* / Q000494:pharmacology*; D001409:Bacillus cereus / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005110:Extracellular Space / Q000187:drug effects / Q000201:enzymology*; D008670:Metals / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000378:metabolism; D012260:Ribonucleases / Q000302:isolation & purification* / Q000494:pharmacology*; D013696:Temperature; D014027:Tobacco Mosaic Virus / Q000187:drug effects*
D000998:Antiviral Agents; D008670:Metals; D012260:Ribonucleases; D010447:Peptide Hydrolases