Linked Life Data

10334846

Source:http://linkedlifedata.com/resource/pubmed/id/10334846

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-7-6
pubmed:abstractText
Proteins that are heavily glycosylated pose unique challenges in their biophysical characterization. In particular, molecular weight analysis is exacerbated by such glycosylation. For example, glyoproteins are refractory to careful mass spectrum analysis and often give anomalous retention times using size exclusion chromatography. We combine several approaches to characterize the molecular weights of the extracellular domains of the glycoproteins CTLA-4 and CD80 using carbohydrate analysis, electrospray mass spectrometry, size exclusion chromatography, and analytical ultracentrifugation. In addition, we have applied a method described previously, using sedimentation equilibrium analysis to calculate the contribution of carbohydrates to the molecular masses of CTLA-4 and CD80. It is important to understand the oligomeric states of these protein domains because the interaction between these lymphocyte receptors plays an important costimulatory role in the Th-cell antigenic response. It is thought that extracellular interactions between these receptors may regulate both the self-association of these receptor proteins and the oligomeric state of the heterocomplex; this regulation has important consequences for potentiating the signaling mechanism between Th-cells and antigen-presenting cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0003-2697
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
286-95
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Molecular weights of CTLA-4 and CD80 by sedimentation equilibrium ultracentrifugation.
pubmed:affiliation
Department of Biology, Haverford College, 370 Lancaster Avenue, Haverford, Pennsylvania 19041, USA. rfairman@haverford.edu
pubmed:publicationType
Journal Article