Linked Life Data

8476928

Source:http://linkedlifedata.com/resource/pubmed/id/8476928

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-5-21
pubmed:abstractText
We have expressed in Escherichia coli the 36 kDa domain of the human poly(ADP-ribose) polymerase. This polypeptide comprises the C-terminal part of the DNA binding domain, as well as the automodification region of the enzyme, but lacks the zinc-finger motifs of the N-terminal region and the C-terminal catalytic domain. By probing the crude E. coli protein extracts with radioactive DNA probes (South-Western blots), we have shown that the 36 kDa domain binds a DNA probe of 222 bp but does not bind a shorter probe of 66 bp. This interaction is stronger when the polypeptide is fused to the 55 kDa catalytic domain of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
1163
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-53
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Expression in Escherichia coli of the 36 kDa domain of poly(ADP-ribose) polymerase and investigation of its DNA binding properties.
pubmed:affiliation
Laboratorie du métabolisme du poly(ADP-ribose), Endocrinologie moléculaire, Centre Hospitalier de l'Université Laval, Québec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't