Linked Life Data

3561388

Source:http://linkedlifedata.com/resource/pubmed/id/3561388

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-5-14
pubmed:abstractText
In partition experiments in aqueous two-phase systems composed of 10% (w/w) dextran (Mr = 500,000) and 7.5% (w/w) poly(ethylene-glycol) (Mr = 6,000) prealbumin and albumin are directed into the dextran-rich phase. Addition of Remazol Yellow GGL covalently bound to poly(ethylene-glycol) causes a transfer of prealbumin and albumin into the poly(ethylene-glycol)-rich phase. This indicates an interaction of both proteins with the dye (affinity phase partitioning). The affinity partitioning effect on prealbumin is markedly increased by an excess of monomeric albumin. This points to an interaction of the two proteins in the presence of the dye. Binding of free Remazol Yellow GGL to prealbumin and albumin was investigated by means of equilibrium dialysis and difference spectroscopy. In respect to prealbumin equilibrium dialysis resulted in the binding of four molecules of the dye to two classes of binding sites with dissociation constants of KH = 3.3 microM and KL = 258 microM respectively whereas albumin was found to bind eight molecules of the dye to two classes of binding sites with KH = 5.8 microM and KL = 282 microM. Similar binding stoichiometries were found by difference spectroscopy. By application of difference spectroscopy and affinity phase partitioning thyroxine and triiodothyronine known as natural ligands of prealbumin and albumin were found to compete with Remazol Yellow GGL for the dye binding sites of the proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-110
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Interaction of the dye Remazol Yellow GGL to prealbumin and albumin studied by affinity phase partition, difference spectroscopy and equilibrium dialysis.
pubmed:publicationType
Journal Article