Linked Life Data

16202231

Source:http://linkedlifedata.com/resource/pubmed/id/16202231

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2005-10-5
pubmed:abstractText
The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing 10(-4) M EDTA. The number of conformational locks and contact areas and amino acid residues of dimers of SOD were obtained by kinetic analysis and biochemical calculation. The cleavage bonds between dimers of SOD during thermal dissociation and type of interactions between specific amino acid residues were also simulated. Two identical contact areas between two subunits were identified. Cleavage of these contact areas resulted in dissociation of the subunits, with destruction of the active centers, and thus, lost of activity. It is suggested that the contact areas interact with active centers by conformational changes involving secondary structural elements.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1225-8687
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
533-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Thermal dissociation and conformational lock of superoxide dismutase.
pubmed:affiliation
Institute of Biochemistry and Biophysics, University of Tehran, Iran.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't