Purification of a novel ribonuclease from dried fruiting bodies of the edible wild mushroom Thelephora ganbajun.
A ribonuclease, with a molecular mass of 30 kDa and a potent inhibitory activity toward HIV-1 reverse transcriptase (IC50=300 nM), was isolated from dried fruiting bodies of the edible wild mushroom Thelephora ganbajun. The ribonuclease exhibited a unique polyhomoribonucleotide specificity, with the highest activity toward poly(U), about 50% and 25% as much activity toward poly(A) and poly(C), respectively, and minimal activity toward poly(G). Unlike other mushroom RNases, the ribonuclease was adsorbed on DEAE-cellulose and Q-Sepharose, and unadsorbed on CM-cellulose. A temperature of 40 degrees C and a pH of 6-7 were required for maximal activity of the enzyme. The enzyme was characterized by an N-terminal sequence without any homology to known proteins.
Wang
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Department of Microbiology, China Agricultural University, Beijing and State Key Laboratory for Agrobiotechnology, Beijing, China. b021770@mailserve.cuhk.edu.hk
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D000363:Agaricales / Q000201:enzymology; D001487:Basidiomycota / Q000201:enzymology*; D002482:Cellulose / Q000737:chemistry; D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange; D003636:DEAE-Cellulose / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D054303:HIV Reverse Transcriptase / Q000037:antagonists & inhibitors; D006863:Hydrogen-Ion Concentration; D020128:Inhibitory Concentration 50; D008970:Molecular Weight; D011061:Poly A / Q000737:chemistry; D011066:Poly C / Q000737:chemistry; D011068:Poly G / Q000737:chemistry; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification*; D012265:Ribonucleotides / Q000737:chemistry; D013696:Temperature
D012265:Ribonucleotides; D011061:Poly A; D011068:Poly G; D011066:Poly C; D002482:Cellulose; D003636:DEAE-Cellulose; D054303:HIV Reverse Transcriptase; D012260:Ribonucleases