Linked Life Data

19865814

Source:http://linkedlifedata.com/resource/pubmed/id/19865814

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-1-21
pubmed:abstractText
The interaction of tumor suppressor p53 with apo-metallothionein (apo-MT) has been carried out using a flow injection-surface plasmon resonance (FI-SPR) instrument. MT was first tethered onto the carboxymethylated dextran film. Via incorporation of glycine-HCl (pH 2) to remove the sequestrated metal ions inherent in MT molecules, a more extended and open structure of apo-MT was formed. Substantial SPR angle shift corresponding to the interaction of wild-type p53 with apo-MT was observed. The interaction was originated from the binding between the free sulfhydryl groups of apo-MT and Zn(2+) of p53 with the binding constant of 1.4 x 10(8) M(-1). The specific binding of p53 to consensus double-stranded DNA was hindered after metal chelation from p53 by apo-MT. Furthermore, inhibition of the interaction between p53 and apo-MT imposed by p53/DNA complex was observed. The fluorescence measurements also revealed the binding of p53 to apo-MT, being consistent with the SPR results. Thus, SPR could potentially serve as an attractive technique for monitoring p53 conformational change and transcriptional activity regulated by the MT/apo-MT couple.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1618-2650
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
395
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2569-75
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Studies of interaction of tumor suppressor p53 with apo-MT using surface plasmon resonance.
pubmed:affiliation
School of Chemistry and Chemical Engineering, Central South University, Changsha, Hunan, 410083, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't