Linked Life Data

1499550

Source:http://linkedlifedata.com/resource/pubmed/id/1499550

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-9-16
pubmed:abstractText
A salt extract of rabbit brain nuclei contains three endoribonucleases, designated RNases Y, A and R, which produce acid-soluble products when incubated at near-neutral pH in the absence of metal ions. RNases Y and A yield products with the monoesterified phosphate at the 3' position, through 2',3'-(cyclic)phosphate intermediates. Oligonucleotides terminating with a 2',3'-(cyclic)phosphate are the end-products of the action of RNase R. Double-stranded substrates are highly resistant to the action of all enzymes. On the basis of limited hydrolysis of end-labelled 5S RNA, the three enzymes differ in their preference for the susceptible phosphodiester bond. Thus, RNase Y hydrolyses preferentially the YpN bond, RNase A the ApN bond and RNase R the RpU bond where R is guanosine in most cases. The advantages and disadvantages of using homopolyribonucleotides and dephosphorylated dinucleotides and trinucleotides in determining various aspects of the specificity of RNases are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
207
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1045-51
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Ribonucleases of diverse specificities in rabbit brain nuclei.
pubmed:affiliation
Laboratory of Biochemistry, School of Chemistry, University of Thessaloniki, Greece.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't