Linked Life Data

6139377

Source:http://linkedlifedata.com/resource/pubmed/id/6139377

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1984-1-27
pubmed:abstractText
Two nucleic acid-dependent ATPases have been isolated from hypotonic extracts of rat liver nuclei and partially characterized. Both enzymes are active with RNA and DNA but are most active with RNA. The most abundant enzyme, ATPase I, is a microheterogeneous, monomeric protein that consists of at least three forms with apparent molecular weights from 53,000 to 60,000. It specifically catalyzes the hydrolysis of ATP (or dATP) to ADP (or dADP) and Pi in the presence of Mg2+ ions and nucleic acid cofactor and has a Km for ATP of 0.15 mM. The other enzyme, ATPase II, consists of a single protein with an apparent molecular weight of 37,000. It catalyzes the hydrolysis of all 4 ribonucleoside triphosphates and dATP to the corresponding nucleoside diphosphate and Pi. For both enzymes, nuclear ribonucleoprotein RNA and cytoplasmic poly(A+) RNA are particularly effective cofactors, while total polysomal RNA (primarily rRNA) is a poor cofactor. The properties of these enzymes make them appear similar to other eukaryotic nucleic acid-dependent ATPases that have been isolated but distinct from the prokaryotic enzyme, RNA synthesis termination factor rho. The biological role of these enzymes is unknown.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14091-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Two ribonucleic acid-dependent nucleoside triphosphate phosphohydrolases from rat liver nuclei.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't