Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-12-18
pubmed:abstractText
The affinity of a panel of neutralizing monoclonal IgGs and their Fab fragments has been measured for the first time with an enveloped type A influenza virus, by surface plasmon resonance (SPR) and the BIAlite instrument. Equilibrium constants could be calculated for four of the five mAbs tested. These were in the nanomolar range. The ranking order was very similar to that obtained with an affinity ELISA, (an equilibrium system) but as others have found, affinities were 2-10-fold lower as measured by SPR (a flow system). No data were obtained with mAb HC58 although it had one of the highest affinities using an ELISA format, and was 28-fold higher than another mAb (HC10) which gave good data by SPR. This may relate to the orientation of its binding on the virion surface. The Kdissoc. of the Fabs was only 3-10-fold higher compared to their IgGs. Fab from the lowest affinity IgG (HC10) could not be measured, possibly because it fell below the threshold for detection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0166-0934
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Determination of affinities of a panel of IgGs and Fabs for whole enveloped (influenza A) virions using surface plasmon resonance.
pubmed:affiliation
Department of Biological Sciences, University of Warwick, Coventry, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't