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Why can hybridoma cells produce large quantities of a single antibody?
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antibody
The four-chain structure of an antibody, or immunoglobulin, molecule. The basic unit is composed of two identical light (L) chains and two identical heavy (H) chains, which are held together by disulfide bonds to form a flexible Y shape. Each chain is composed of a variable (V) region and a constant (C) region.
Hybridoma cells are capable of producing large quantities of a specific monoclonal antibody because they combine the functional strengths of two different cell types through cell fusion:
- Antibody Production: The hybridoma inherits the ability to secrete a specific, desired antibody from a normal B cell (typically harvested from the spleen of an immunized mouse).
- Indefinite Proliferation: The hybridoma retains the capacity of its myeloma (cancerous) component to multiply indefinitely in culture.
By fusing these cells, researchers create a stable, immortalized cell line that continuously secretes a single, identifiable type of immunoglobulin. This technique, developed by Georges Köhler and César Milstein, allows for the reliable production of monoclonal antibodies in quantities sufficient for medical diagnostics, research, and therapy.1