A ribonuclease from the wild mushroom Boletus griseus.
A ribonuclease (RNase) with a molecular mass of 29 kDa and cospecific for poly A and poly U was isolated from fruiting bodies of the mushroom Boletus griseus. Its N-terminal sequence exhibited some similarity to those of RNases from the mushrooms Irpex lacteus and Lentinus edodes. The RNase was adsorbed on diethylaminoethyl-cellulose, Q-Sepharose, and Affi-gel blue gel and was unadsorbed on CM-cellulose. The enzyme exhibited a temperature optimum between 60 and 70 degrees C and a pH optimum at 3.5.
State Key Laboratory of Agrobiotechnology, Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China.
Hexiang
H
Wang
T B
TB
Ng
D000363:Agaricales / Q000201:enzymology*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D012343:RNA, Transfer / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism*; D013696:Temperature
D012343:RNA, Transfer; D012260:Ribonucleases