Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-1-7
pubmed:abstractText
Monoclonal antibodies (Mabs) directed against cell surface determinants and conjugated to fluochromes, radionuclids or drugs are of increasing importance in cell and tumor biology as well as in clinical oncology. Many of the applications of Mab require precise and quantitative information regarding the molecular interactions of labeled antibody with the respective antigen expressed on the cell surface. These interactions are characterized by the association rate constant (ka), the dissociation rate constant (kd) and the antibody affinity constant (K). The immunoreactive fraction (IRF) of the labeled antibody molecules directly influences these parameters. IRF is usually reduced below 100% by antibody purification and labeling procedures and, in case of radiolabeled antibodies, by radiation damage during antibody storage. Besides the calculation of kinetic parameters, IRF should, therefore, be determined for the quality control of any antibody preparation before experimental or clinical application. Commonly used methods for measuring IRF are based on radioimmunoassays (RIA) on intact cells performed under antigen excess. However, especially with Mabs directed against cell surface antigens expressed in small numbers per cell and for displaying low affinity constants, these assays often give unsatisfactory results. We have, therefore, established a method which permits us to determine IRF, ka, kd and K for an 125I-labeled Mab with precision even in the absence of antigen excess.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
175-83
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Determination of immunoreactive fraction and kinetic parameters of a radiolabeled monoclonal antibody in the absence of antigen excess.
pubmed:affiliation
Institute of Cell Biology (Cancer Research), West German Cancer Center Essen, University of Essen Medical School, F.R.G.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't