title: Purification and properties of a nuclease from the fruit body of Tricholoma matsutake.
abstract: 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.
authors.affiliation: Faculty of Bioresource Science, Akita Prefectural University, Japan.
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Hatakeyama
authors.forename: Kouichi
authors.initials: K
authors.lastname: Mizuno
authors.forename: Shin-ichi
authors.initials: S
authors.lastname: Kurosawa
mesh_terms: 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*
chemical_list: D012313:RNA; D004247:DNA; D004950:Esterases