English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

We report kinetic studies on the reaction of a latex agglutination immunoassay used to quantify phenytoin in serum. In this assay, polystyrene particles with a covalently attached analog of phenytoin react with an antiphenytoin monoclonal antibody to form light-scattering aggregates, with the rate of this reaction being decreased by addition of phenytoin from sample. In the absence of free (sample) phenytoin, this reaction did not exhibit a maximum rate of agglutination in the presence of excess antibody, i.e., an equivalence point. Furthermore, agglutination was inhibitable by free phenytoin even when the latter was added after agglutination of particles with antibody had begun. Most significantly, the immunoagglutination proceeded in an identical fashion with monovalent F(ab) fragment. These data are consistent with low-affinity immunospecific particle-antibody complexation, which then induces colloidal aggregation, without requiring immunospecific bridging by antibody molecules. The described mechanism is not generalizable to all latex agglutination immunoassays, although disturbance of colloidal stability may be a component in most assays.

Kinetics and proposed mechanism of the reaction of an immunoinhibition, particle-enhanced immunoassay