Linked Life Data

1993052

Source:http://linkedlifedata.com/resource/pubmed/id/1993052

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-3-8
pubmed:abstractText
A novel 55 kDa DNA-binding protein (p55) was purified from HeLa cell nuclear extracts to apparent homogeneity by conventional chromatography coupled with DNA-affinity chromatography. The DNA-binding activity of p55, followed by band mobility shift and Southwestern assays, was enriched 800-fold. This relatively abundant protein was shown to bind nonspecifically to DNA. When added to nuclear extracts, p55 enhanced 2-fold the in vitro transcription of CAT reporter gene driven by the SV40 promoter. The sequence of the N-terminal 20 amino acid residues of purified p55 was determined as APSTPLLTV(P)G(S)EGLYMVNG, homologies could be found when compared to protein sequences available in all databanks.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
542-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Purification of a novel 55 kDa HeLa cell nuclear DNA-binding protein.
pubmed:affiliation
Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't