Linked Life Data

10350605

Source:http://linkedlifedata.com/resource/pubmed/id/10350605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-7-12
pubmed:abstractText
Luminescence techniques have been used to investigate the interaction of GroEL with polylysine tagged with a fluorescent probe. The fluorescence emitted by anthraniloyl-polylysine, upon excitation at 320 nm, is enhanced by the addition of stoichiometric amounts of GroEL. The equilibrium dissociation constant of the complex (Kd=50 nM) was determined by fluorometric titrations. The rate and extent of recovery of the catalytic activity of denatured mitochondrial malate dehydrogenase, assisted by GroEL, is influenced by either polylysine or anthraniloyl-polylysine. It is suggested that interaction of the positively charged poly-amino acid with the apical domain of GroEL prevents binding of the unfolded protein substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
1431
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
282-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Binding of polylysine to GroEL. Inhibition of the refolding of mMDH.
pubmed:affiliation
Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, General Office, GH 602, Hung Hom, Kowloon, Hong Kong, China.
pubmed:publicationType
Journal Article