A novel ribonuclease from fruiting bodies of the common edible mushroom Pleurotus eryngii.
A ribonuclease with a temperature optimum of about 70 degrees C and a pH optimum of 6.5 was isolated from fruiting bodies of the mushroom Pleurotus eryngii. The ribonuclease was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and S-Sepharose. It possessed a molecular mass of 16 kDa, and exhibited higher ribonucleolytic activity toward poly A and poly G and lower ribonucleolytic activity toward poly C and poly U. Its N-terminal sequence was distinctly different from those of other mushroom ribonucleases, and resembled that of Pleurotus tuber-regium only by 40%. Furthermore, its thermostability characteristics, polyhomoribonucleotide specificity and molecular mass were dissimilar to those of other mushroom ribonucleases.
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Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China. biochemistry@cuhk.edu.hk
Wang
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D000595:Amino Acid Sequence; D004795:Enzyme Stability; D048690:Fruiting Bodies, Fungal / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D020076:Pleurotus / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification; D013045:Species Specificity; D013379:Substrate Specificity; D013696:Temperature
D012260:Ribonucleases