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#12498197   // Save this To Up

In situ single-molecule detection of antibody-antigen binding by tapping-mode atomic force microscopy.

We performed in situ detection of specific and nonspecific binding during immunoreaction on surfaces at the same location before and after analyte was injected using tapping-mode atomic force microscopy (TM-AFM) in liquid and demonstrated the ability of TM-AFM to monitor the occurrence of single-molecule binding events and to distinguish nonspecific from specific binding by examining topographical change. Two antigen/antibody pairs were investigated: chorionic gonadotropin (hCG)/mouse monoclonal anti-hCG and goat IgG (anti-intact hCG)/ mouse monoclonal anti-goat IgG. Antibody (or antigen) molecules were covalently immobilized on uniform mixed self-assembled monolayers (SAMs) terminated with carboxylic acid and hydroxyl groups. Mixed SAMs allow the control of the density of immobilized antibody (or antigen) on surfaces to achieve the detection of individual antigens, antibodies, and antigen/antibody complexes. This in situ TM-AFM-based detection method allows the single-molecule detection of antigen/antibody binding under near-physiological environment and the distinction of nonspecific from specific binding. It could be extended into a microarray.

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Use of synthetic canine relaxin to develop a rapid homologous radioimmunoassay.

Canine relaxin (cRlx) was synthesized by a combination of solid-phase methods and sequential site-directed disulfide bond formation. Proof that the intended molecule had been synthesized was obtained by analytical HPLC of the intact and reduced molecule, by amino acid and sequence analysis, and by receptor binding and in vivo mouse interpubic ligament bioassays. Antisera to synthetic cRlx were raised in six male rabbits; these cross-reacted with relaxins of other species, but not with insulin, LH, FSH, hCG, or prolactin (PRL). Three of the antisera neutralized relaxin-induced interpubic ligament formation in estrogen-primed mice in vivo. A new homologous cRlx RIA was developed through the use of rabbit antiserum 79888, synthetic cRlx for standards and 125l-labeled trace, and a goat anti-rabbit lgG-polyethylene glycol precipitant. The new RIA can be completed in 26 h and has a sensitivity of 0.195-0.39 ng cRlx/tube. Intra- and interassay coefficients of variation were 3% and 12.5%. During pregnancy in bitches, serum cRlx rose to about 10 micrograms/ml. Immunoactive cRlx was also detected in serum, colostrum, and milk of lactating bitches, but not in large volumes (100-300 microliters) of serum of pseudopregnant or estrous bitches. Immunoreactive cRlx was also found in seminal plasma, but not in serum, of male dogs. The new homologous cRlx RIA is simple, rapid, sensitive, and specific, and will be used in future studies of canine relaxin physiology.

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Goat antibodies to amino acid sequences of human chorionic gonadotropin (hCG)

Human chorionic gonadotropin, its two subunits and its conjugate with thyroglobulin were used for immunization. The strongest immunogens were demonstrated to be the intact hormone and beta subunit, the weakest was alpha subunit. Using three peptides corresponding to hormone subunits coupled to Sepharose 4B various antibodies were isolated from goat antiserum by immunoaffinity chromatography. Specificity of the purified antibody preparations was studied. It was demonstrated that enzyme linked immunosorbent assay with two goat antibodies--one for coating of microtiter plates and the other one conjugated with peroxidase--is suitable for sensitive assays of both human chorionic gonadotropin and luteinizing hormone. Specific and sensitive assays were performed using combination of goat antibody anti-122-145-beta hCG and monoclonal antibody anti-alpha hCG.

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Development and validation of a choriogonadotropin beta-subunit radioimmunoassay for serum choriogonadotropin using commercially available components.

A sensitive, specific, accurate and precise radioimmunoassay procedure developed for the beta-subunit of serum choriogonadotropin (hCGbeta) is described. 1. The assay employs an anti-hCGbeta (rabbit) serum generated against hCGbeta, highly purified intact choriogonadotropin (hCG) as standard, and [125I]hCG as the radioactive ligand. The antibody-bound hCG was separated from the free hormone by the addition of goat anti-rabbit gamma-globulin. 2. The detection limit of the assay was approximately 75 microIU hCG which corresponds to a serum concentration of approximately 0.75 mIU/mL. 3. Cross reactivity studies performed with human luteinizing hormone (hLH) and human thyroid-stimulating hormone (hTSH) indicated minimal interferences from these structurally similar glycoproteins. Parallel dose-response curves were demonstrated between dilutions of sera with elevated hCG concentrations and the standard reference preparation. A non-specific binding of less than 2.5% of the total [125I]hCG was routinely observed. 4. The analytical recovery of hCG added to human sera varied from 94 to 110%, with a mean recovery of 101%. 5. The inter-assay variation was determined by assaying (n=30) 3 different quality control pools. The following data were obtained: X1=4.6 +/- 0.5 mIU/mL (CV=10.9%); X2=8.1 +/- 0.9 mIU/mL (CV=11.1%); and X3=36.8 +/- 2.8 mIU/mL (CV=7.6%). 6. The clinical data collected from subjects with trophoblastic disease agreed with previously published studies. All of the reagents are available commercially.

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