Monoclonal antibodies to bovine serum albumin: Affinity and specificity determinations

1988 ◽  
Vol 25 (1) ◽  
pp. 7-15 ◽  
Author(s):  
Guillemette A. Morel ◽  
David M. Yarmush ◽  
Clark K. Colton ◽  
David C. Benjamin ◽  
Martin L. Yarmush
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

scholarly journals Heterologous screening of hybridomas for the development of broad-specific monoclonal antibodies against deoxynivalenol and its analogues

2014 ◽  
Vol 7 (3) ◽  
pp. 257-265 ◽  
Author(s):  
Y. Guo ◽  
M. Sanders ◽  
A. Galvita ◽  
A. Heyerick ◽  
D. Deforce ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Horseradish Peroxidase ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Simultaneous Detection ◽  
Cross Reactivity ◽  
Efficient Approach ◽  
Selection For ◽  
Similar Affinity

Hapten heterology was introduced into the steps of hybridoma selection for the development of monoclonal antibodies (MAbs) against deoxynivalenol (DON). Firstly, a novel heterologous DON hapten was synthesised and covalently coupled to proteins (i.e. bovine serum albumin (BSA), ovalbumin and horseradish peroxidase) using the linkage of cyanuric chloride (CC). After immunisation, antisera from different DON immunogens were checked for the presence of useful antibodies. Next, both homologous and heterologous enzyme-linked immunosorbent assays were conducted to screen for hybridomas. It was found that heterologous screening could significantly reduce the proportion of false positives and appeared to be an efficient approach for selecting hybridomas of interest. This strategy resulted in two kinds of broad-selective MAbs against DON and its analogues. They were quite distinct from other reported DON-antibodies in their cross-reactivity profiles. A unique MAb 13H1 derived from DON-CC-BSA immunogen could recognise DON and its analogues in the order of HT-2 toxin ≯ 15-acetyl-DON ≯ DON ≯ nivalenol, with IC50 ranging from 1.14 to 7.69 μg/ml. Another preferable MAb 10H10 generated from DON-BSA immunogen manifested relatively similar affinity to DON, 3-acetyl-DON and 15-acetyl-DON, with IC50 values of 22, 15 and 34 ng/ml, respectively. This is the first broad-specific MAb against DON and its two acetylated forms and thus it can be used for simultaneous detection of the three mycotoxins.

Immunoregulation of the anti-bovine serum albumin response by polyclonal and monoclonal antibodies

1983 ◽  
Vol 80 (2) ◽  
pp. 279-287 ◽  
Author(s):  
Nancy J. Krieger ◽  
Amadeo Pesce ◽  
J.Gabriel Michael
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Radioimmunoassay of osteocalcin with polyclonal and monoclonal antibodies.

1989 ◽  
Vol 35 (7) ◽  
pp. 1408-1415 ◽  
Author(s):  
M J Power ◽  
J P Gosling ◽  
P F Fottrell
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Normal Range ◽  
Serum Samples ◽  
Wide Range ◽  
Assay Precision

Abstract We have developed and thoroughly validated radioimmunoassays (RIAs) for osteocalcin in plasma and serum, demonstrating independence of volume and determining the recovery of added standard and within- and between-assay precision. Antibodies were raised in rabbits and mice by immunization with either osteocalcin adsorbed to polyvinylpyrrolidone or osteocalcin conjugated to bovine serum albumin. In both species, use of the conjugated osteocalcin was more efficacious. Correlation of the results obtained when groups of plasma or serum samples were analyzed by RIAs with different antibodies (two polyclonal and one monoclonal) indicated that the normal range observed for osteocalcin concentrations in serum depends on the antibody used. These findings may account for the wide range of "normal" osteocalcin values reported by different groups.

scholarly journals Characterization and immunocytochemical application of monoclonal antibodies against enkephalins.

1984 ◽  
Vol 32 (9) ◽  
pp. 947-957 ◽  
Author(s):  
A C Cuello ◽  
C Milstein ◽  
R Couture ◽  
B Wright ◽  
J V Priestley ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Endogenous Peptides ◽  
Beta Endorphin ◽  
Suitable Tool

Monoclonal antibodies were produced following immunization of mice with either [Leu5]enkephalin-bovine serum albumin or [Met5]enkephalin-keyhold limpet hemocyanin conjugates. Two monoclonal antibodies coded NOC1 and NOC2, respectively, were derived. These monoclonal antibodies did not discriminate between Leu- and Met-enkephalin in either radioimmunoassay or immunocytochemistry. NOC1 was characterized in detail. In radioimmunoassay NOC1 displayed about 40% crossreactivity with C-terminal extended Met-enkephalin hexapeptides and 7% with the extended heptapeptide (-Arg-Phe-OH), but did not recognize other endogenous peptides. In immunocytochemistry the NOC1 and NOC2 recognized all well-established "enkephalin immunoreactive sites," but they did not bind to areas known to contain beta-endorphin or high levels of pro-enkephalin. NOC1 was shown to be a suitable tool to demonstrate enkephalin immunoreactive sites by radioimmunocytochemistry utilizing both internally and externally labeled monoclonal antibodies.

Production of Monoclonal Antibodies against Diquat and Its Enzyme-Linked Immunosorbent Assay

1993 ◽  
Vol 33 (2) ◽  
pp. 117-120 ◽  
Author(s):  
B Wu ◽  
M Nagao ◽  
K Terazawa ◽  
T Takatori ◽  
H Akabane
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunosorbent Assay ◽  
Bovine Serum ◽  
Clinical Sample ◽  
Enzyme Linked Immunosorbent Assay ◽  
Spleen Cells ◽  
Myeloma Cells ◽  
Toxicological Analysis

Monoclonal antibodies(MoAbs) very specific to diquat (DQ) were produced. An immunogen was synthesized by binding DQ to bovine serum albumin via a diazo-coupled derivative. BALB/c mice were immunized i.p. monthly with 0.25mg of the immunogen for five months. Their spleen cells were fused with P3U1 myeloma cells and hybridoma clones secreting MoAbs were obtained. Two MoAbs were selected and subtyped to be IgM and IgG3. The MoAbs recognized DQ but did not bind to paraquat and other analogues at all. A datum obtained from a clinical sample demonstrates that an enzyme-linked immunosorbent assay system using one of the MoAbs is useful in the practice of toxicological analysis.

scholarly journals Bovine serum albumin as an immunogenic carrier facilitating the development of hapten-specific monoclonal antibodies

2020 ◽  
Author(s):  
Ruotong Zhao ◽  
Mingjun Jiang
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Fetal Bovine Serum ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Common Misconception ◽  
Fetal Bovine

AbstractThere is a common misconception that the generation of hapten-specific monoclonal antibodies (mAbs) requires the use of a heterologous conjugate to ensure carrier-specific antibodies not being detected. In this study, salbutamol (SAL) was used as a model hapten to exhibit the benefits of bovine serum albumin (BSA) as a carrier for developing hapten-specific mAbs. SAL-BSA conjugate would serve as both an immune antigen and a screening antigen during the preparation of SAL-specific mAbs. Six hybridomas were identified to secret mAbs specific for free SAL with minor or negligible cross-reactivity with other β-agonists. Meanwhile, none of hybrodomas secreting anti-BSA antibodies were screened out even though the fetal bovine serum (FBS) added to the medium decreased from 10% to 1% (v/v). Based on one of the six mAbs, 3F12, a direct competitive enzyme-linked immunosorbent assay (dcELISA) was developed for meausring SAL. Under the optimized assay, the quantitative working range was from 312.5 to 20,000 pg/mL (R2 = 0.9959), with a limit of detection (LOD) of 142.9 pg/mL. The results showed that BSA is an efficient and suitable protein carrier for facilitating the development of hapten-specific mAbs.

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