Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-4-11
pubmed:abstractText
The biologically active form of interferon gamma (IFN-gamma) is a dimer consisting of two identical non-covalently bound polypeptide chains. We have studied spectroscopically the dimer-monomer dissociation equilibrium of human recombinant IFN-gamma and have found that the monomers possess approximately 50% lower Trp quantum yield than the dimers [Boteva et al. Biochemistry 1996;35:14825]. In the present study we characterise the conformational properties of the two states--monomeric and dimeric, and analyse the effects of the salt composition of human blood plasma, physiological cations K+, Na+, Ca2+ and Mg2+ and mechanical stress on the dimer-monomer equilibrium. A medium with electrolyte composition of human blood plasma increases both the association and dissociation rate constants without shifting significantly the dimer-monomer equilibrium. The physiological cations shift the equilibrium towards dissociation of dimers into monomers by lowering the activation energy and the free energy of the process thus decreasing the stability of IFN-gamma. Mechanical stress caused by stirring of the protein solution reduces irreversibly the Trp fluorescence by 75-80% and decreases significantly the alpha-helical content and favours the aggregation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
357-62
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Factors affecting the dissociation and aggregation of human interferon gamma.
pubmed:affiliation
CNR Centre of Metalloproteins, Department of Biology, University of Padua, Italy.
pubmed:publicationType
Journal Article