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Details van artikel 17 van 132 gevonden artikelen
| Titel: |
Determination of dissociation constants of Anti-ALP monoclonal antibodies by an ELISA – based method |
| Auteur: |
Naseri, Mohsen Moazzeni, Mohammad Pourfathollah, Ali Akbar Fatemeh, Rahbarizadeh |
| Verschenen in: |
Human antibodies |
| Paginering: | Jaargang 23 (2015) nr. 1-2 pagina's 1-5 |
| Jaar: |
2015-03-26 |
| Inhoud: |
BACKGROUND: Dissociation constant (K_{d}) is of major significance in immunoassay. Since affinity may be influenced by the immunoassay methodology it is important to determine this parameter under the condition of the assay used. OBJECTIVE: To employ a rapid and simple ELISA- based method for measuring dissociation constants of two Alkaline Phosphatase (ALP) specific MAbs (A_{1}G_{8}F_{7} and A_{1}G_{9}G_{3}) established in our laboratory. METHODS: A simple and rapid method on enzyme- linked immunosorbent assay (ELISA) was developed for measuring the dissociation constant of antibody – antigen reactions. In this method the ability of increasing amounts of antigen to bind to antibody measured in the fluid phase. RESULTS: Based on the data obtained from this study, the dissociation constants of A_{1}G_{8}F_{7} and A_{1}G_{9}G_{3} MAbs were 3.8 × 10^{-9} and 4.3 × 10^{-9} M, respectively. CONCLUSIONS: A_{1}G_{8}F_{7} and A_{1}G_{9}G_{3} MAbs with reasonably high affinity are suggested for used in very immunoassay such as ELISA, immunocytochemistry and immunihistochemistry (APAAP method). |
| Uitgever: |
IOS Press |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
Details van artikel 17 van 132 gevonden artikelen
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