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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-5-1
pubmed:abstractText
From the fresh sclerotia of the mushroom Pleurotus tuber-regium, a potent homodimeric ribonuclease exhibiting a molecular weight of 29 kDa in FPLC-gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis was isolated. The protein was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel, CM-cellulose and Mono S. It manifested strong ribonucleolytic activity toward Poly G, slight activity toward Poly U and Poly A, and minimal activity toward Poly C. Its optimal pH was determined to be 6.5 when yeast transfer RNA was used as substrate. Its ribonucleolytic activity was resistant to heating at 100 degrees C for 30 min but was inhibited by a number of salts. The protein inhibited cell-free translation in a rabbit reticulocyte lysate with an IC50 of 0.09 nM. Three out of the four amino acid residues at the active site (positions 38-41) of P. ostreatus ribonuclease, YNNF, were also found at positions 17-20 in the P. tuber-regum RNase. However, unlike P. ostreatus RNase, no cysteine residues were detected in the N-terminal sequence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
483-90
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Purification and characterization of a potent homodimeric guanine-specific ribonuclease from fresh mushroom (Pleurotus tuber-regium) sclerotia.
pubmed:affiliation
Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China.
pubmed:publicationType
Journal Article