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Detection of Heavy Metals by Immunoassay: Optimization and Validation of a Rapid, Portable Assay for Ionic Cadmium
An immunoassay is described that measured Cd(II) in aqueous samples at concentrations from approximately 7 to 500 ppb. The assay utilized a monoclonal antibody that bound tightly to a
Metal Binding Properties of a Monoclonal Antibody Directed toward Metal-Chelate Complexes*
A monoclonal antibody that recognizes cadmium-EDTA complexes has been produced by the injection of BALB/c mice with a metal-chelate complex covalently coupled to a carrier protein. The ability of
Comparison of binding characteristics and in vitro activities of three inhibitors of vascular endothelial growth factor A.
Biacore studies and SV-AUC solution studies show that aflibercept does not bind with higher affinity than ranibizumab to VEGF as recently reported,4 and both inhibitors appeared to be equipotent with respect to their ability to inhibit V EGF function.
Binding properties of a monoclonal antibody directed toward lead-chelate complexes.
A monoclonal antibody (2C12) that recognizes a Pb(II)-cyclohexyldiethylenetriamine pentaacetic acid complex was produced by the injection of BALB/c mice with a P b( II)-chelate complex covalently coupled to a carrier protein by measuring equilibrium dissociation constants.
Immunoassays for metal ions
Abstract Antibodies that recognize chelated forms of metal ions have been used to construct immunoassays for Cd(II), Hg(II), Pb(II), and Ni(II). In this paper, the format of these immunoassays is
Custom-Designed Affinity Capture LC-MS F(ab')2 Assay for Biotransformation Assessment of Site-Specific Antibody Drug Conjugates.
The newly developed affinity capture LC-MS F(ab')2 assay provides more detailed and accurate information on ADC biotransformations in vivo, enabling analysis of low-dose, labile, and complex site-specific ADCs with linker-drug conjugated in the Fab region.
Novel monoclonal antibodies with specificity for chelated uranium(VI): isolation and binding properties.
The synthesis of 5-isothiocyanato-1,10-phenanthroline-2,9-dicarboxylic acid is described and its use in the generation and functional characterization of a group of monoclonal antibodies that recognize the most soluble and toxic form of uranium, the hexavalent uranyl ion.
Allosteric binding properties of a monoclonal antibody and its Fab fragment.
These data are interpreted in terms of a model in which aminobenzyl-DTPA and its complexes bind both to the antigen binding site and to multiple charged sites on the surface of the compact immunoglobulin; and the bound, highly charged ligands interact in a complicated fashion through the apolar core of the folded antibody.
Monoclonal antibodies against surface antigens of Pasteurella multocida strain P-1059.
Four monoclonal antibodies were developed against serotype 3:A, P-1059 strain of Pasteurella multocida to screen hybridomas producing antibodies to either a surface protective (2.5 S) or lipopolysaccharide (LPS) antigen.