Purification and properties of a nuclease from the fruit body of Tricholoma matsutake.
A nuclease was purified from the fruit body of Tricholoma matsutake. The molecular mass was 38 kDa. The optimum pH of the nuclease was about 8.0. Its activity was inhibited by GTP. The nuclease cleaved RNA and heat-denatured DNA endonucleolytically to produce 5'-mononucleotide, and showed 3'-nucleotidase activity. The amino acid sequence up to seven amino acids from the N-terminus was NH(2)-APPPSSN.
Hatakeyama
Tomoyuki
T
Faculty of Bioresource Science, Akita Prefectural University, Japan.
Mizuno
Kouichi
K
Kurosawa
Shin-ichi
S
D004247:DNA / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004950:Esterases / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D012313:RNA / Q000378:metabolism; D013696:Temperature; D055439:Tricholoma / Q000201:enzymology*
D012313:RNA; D004247:DNA; D004950:Esterases