Linked Life Data

1530627

Source:http://linkedlifedata.com/resource/pubmed/id/1530627

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-10-22
pubmed:abstractText
Rb protein was purified from recombinant baculovirus-infected Sf9 cells to apparent homogeneity by a simple solubilization and by immunoaffinity column chromatography. It was mainly obtained as p110Rb, the underphosphorylated form of the Rb protein family. This p110Rb was shown to form a specific complex in vitro with SV40 Tag and to bind to double or single stranded DNA. It could also affect Tag helicase activity in a biphasic-dose dependent manner, due to these two biochemical functions. This purification procedure provides sufficient amounts of native Rb protein to further elucidate its role as an anti-oncogene protein and a negative regulator of the cell cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
187
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
697-702
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Efficient purification of a full length and biochemically active p110Rb, the retinoblastoma gene product.
pubmed:affiliation
Laboratory of Cancer Cell Biology, Nagoya University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't