Linked Life Data

9617834

Source:http://linkedlifedata.com/resource/pubmed/id/9617834

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1998-6-23
pubmed:abstractText
In previous publications we have discussed the stabilization mechanism of hydration forces as applied to the development of latex agglutination tests. We describe here how we have obtained stable and reactive IgG-latex conjugates in a high-ionic-strength reaction buffer. To this end we have made agglutination tests with polystyrene beads sensitized with IgG, measuring the immunoaggregation reaction with human C-reactive protein in a stopped-flow nephelometer. The results are compared to those obtained with a F(ab')2-latex conjugate with similar antibody molecule coverage. Adsorption isotherms of F(ab')2 and IgG on latex at pH 7.2 were obtained to study the affinity of these antibodies for the surface. The results of the electrokinetic characterization of the antibody-latex conjugates agree satisfactorily with those obtained from stability studies. This research throws light upon the use of hydration forces as a new approach to stabilizing immunoassay reagents that are colloidally unstable in physiological reaction buffers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
211
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
87-95
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Particle enhanced immunoassays stabilized by hydration forces: a comparative study between IgG and F(ab)2 immunoreactivity.
pubmed:affiliation
Department of applied Physics, Faculty of Sciences, Campus Fuenteneuva, University of Granada, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't