Linked Life Data

8144588

Source:http://linkedlifedata.com/resource/pubmed/id/8144588

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1994-5-5
pubmed:abstractText
A double-stranded RNA adenosine deaminase that catalyzes the conversion of adenosines to inosines in duplex RNA substrates was purified to near homogeneity from Xenopus laevis eggs. The final specific activity was approximately 2.0 nmol of inosine min-1 mg-1 at 25 degrees C and pH 7.9 with a 794-base pair RNA substrate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a single major approximately 120-kDa protein band by silver staining. The purified enzyme migrated with an apparent molecular mass of 90 +/- 10 kDa during high performance liquid chromatography. Gel filtration of the partially purified enzyme gave an apparent molecular mass of 210 +/- 20 kDa, suggesting that the enzyme may dimerize or associate with other cellular components. Substrate modification was inhibited by excess substrate, thiol reagents, heparin, and moderate concentrations of monovalent cations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9933-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Purification of the Xenopus laevis double-stranded RNA adenosine deaminase.
pubmed:affiliation
Department of Biochemistry, University of Utah, Salt Lake City 84132.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't