[Isolation and some properties of a nonspecific extracellular ribonuclease of Aspergillus clavatus].
RNase has been isolated from the homogenate of the Aspergillus clavatus mycelium by gel filtration through Sephadex G-75, chromatography on CM-cellulose and DEAE-cellulose. By gel filtration and electrophoresis in polyacrylamide gel the preparation has been shown to be homogeneous. The enzyme is acid protein with the isoelectric point at pH 4.4 and molecular weight of 27,000. RNase has pH optimum at 6.0--6.2 and temperature optimum 60 degrees for RNA action. The enzyme splits RNA completely in the absence of metal ions. Ions Zn2+, Cu+2, Ag+1 and Ni+2 at a concentration of 10(-4) M are strong inhibitors of RNase activity.
D001230:Aspergillus / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D007526:Isoelectric Point; D008970:Molecular Weight; D012313:RNA / Q000378:metabolism; D012260:Ribonucleases / Q000032:analysis / Q000302:isolation & purification*; D013053:Spectrophotometry
D003470:Culture Media; D012313:RNA; D012260:Ribonucleases
Vydelenie i nekotorye svoĭstva nespetsifichnoĭ vnekletochnoĭ ribonukleazy Aspurgillus clavatus