The influence of antibody affinity on the radioallergosorbent test (RAST) and in vitro histamine release: Studies with hapten-specific monoclonal IgE antibodies

Download
  1. Get@NRC: The influence of antibody affinity on the radioallergosorbent test (RAST) and in vitro histamine release: Studies with hapten-specific monoclonal IgE antibodies (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1016/0022-1759(86)90365-0
AuthorSearch for: ; Search for: ; Search for:
TypeArticle
Journal titleJournal of Immunological Methods
Volume89
Issue2
Pages249255; # of pages: 7
Subjectanibody affinity; monoclonal anitbody; IgE; RAST; histanmine release
AbstractFour murine monoclonal IgE antibodies specific for the hapten, 4-hydroxy-3-nitrophenylacetyl (NP), had been previously found to be heteroclitic in nature in that they bound the crossreacting hapten, 4-hydroxy-3-iodo-5-nitrophenylacetyl (NIP), with greater affinity than NP. The influence of antibody affinity on the results of two commonly used assays for IgE, namely the radioallergosorbent test (RAST) and histamine release from rat peritoneal mast cells, was studied using these antibodies. In general, in agreement with previous reports, it was found that affinity influences both RAST and histamine release; however, the affinity constants deduced from equilibrium dialysis measurements for the reactions with monovalent haptens were not directly related to the activities of the antibodies as reflected in assays using multivalent hapten protein conjugates.
Publication date
LanguageEnglish
Peer reviewedYes
NRC publication
This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

NRC number1682
NPARC number9742064
Export citationExport as RIS
Report a correctionReport a correction
Record identifier0ec967c2-3fb9-46a5-9b70-784e135e636c
Record created2009-07-17
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)