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The comparison of the ability of monoclonal antibodies directed to different proteins (human IgG, human myoglobin and HRP) and bispecific antibodies derived thereof to bind antigens immobilized on a surface of a solid phase.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Dmitriev, Dmitriy A. Massino, Yulia S. Segal, Olga L. Smirnova, Maria B. Kolyaskina, Galina I. |
| Copyright Year | 2001 |
| Abstract | BACKGROUND Bindings of mouse monoclonal antibodies (mAbs) and affinity purified bispecific antibodies (bAbs), derived thereof, to antigens adsorbed on immunoplates have been compared, using ELISA and RIA methods. METHODS The analysed panel of antibodies included mAbs specific to human myoglobin (Mb), human IgG (hIgG) and horseradish peroxidase (HRP) and biologically produced bAbs with double specificity to Mb and HRP, and to hIgG and HRP. RESULTS The degree of difference between different mAbs and corresponding bAbs varied markedly from antibody to antibody, depending on whether the parental mAbs could bind immobilized antigens bivalently. The observed equilibrium binding constant (K(obs)) for anti-HRP mAbs was 21-38 times higher that of anti-HRP site of bAbs (anti-hIgG/HRP or anti-Mb/HRP, respectively), due to bivalent binding of mAbs. Anti-Mb mAbs also bound bivalently with immobilized Mb. On the contrary, anti-hIgG mAbs bound monovalently with immobilized hIgG in the same conditions. The avidity of anti-Mb/HRP bAbs increased, if both antigens were simultaneously adsorbed on a solid phase. CONCLUSIONS The obtained data indicate that the use of bAbs in heterogeneous immunoassays instead of traditional mAb-enzyme conjugates hardly can provide the significant gain in assay performance if parental mAbs bind bivalently. |
| Starting Page | 57 |
| Ending Page | 71 |
| Page Count | 15 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://istina.msu.ru/download/75175436/1gSg4I:cZbO_nMbiGHFq0vhj5YXGXkbYCw/ |
| PubMed reference number | 11408007v1 |
| Volume Number | 309 |
| Issue Number | 1 |
| Journal | Clinica chimica acta; international journal of clinical chemistry |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Affinity Enzyme-Linked Immunosorbent Assay Genetic Heterogeneity HIV Antibodies Horseradish Peroxidase Immunoassay method Immunoglobulin G, Human Immunostimulating conjugate (antigen) MB gene Monoclonal Antibodies Radioimmunoassay |
| Content Type | Text |
| Resource Type | Article |