Isolation of a ribonuclease from fruiting bodies of the wild mushroom Termitomyces globulus.
A ribonuclease, with a molecular mass of 13 kDa and a ubiquitin-like N-terminal sequence, has been isolated from fruiting bodies of the mushroom Termitomyces globulus. The ribonuclease demonstrated ribonucleolytic activity toward poly A, poly C, poly G and poly U, with the activity toward poly A and poly C being much higher than that toward poly G and poly U. The ribonuclease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-Sepharose. The enzyme required a temperature of 70 degrees C for expression of maximal activity. However, the enzyme expressed nearly the same optimal activity over a wide pH range of 5.0-8.0.
D000363:Agaricales / Q000201:enzymology*; D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011061:Poly A / Q000378:metabolism; D011066:Poly C / Q000378:metabolism; D011068:Poly G / Q000378:metabolism; D011072:Poly U / Q000378:metabolism; D012260:Ribonucleases / Q000032:analysis / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014227:Triazines / Q000737:chemistry
D014227:Triazines; D011061:Poly A; D011068:Poly G; D011072:Poly U; D011066:Poly C; C012842:Cibacron Blue F 3GA; D012260:Ribonucleases