Abstract
The enzyme 20-α-hydroxysteroid dehydrogenase (20-α-HSD) was purified from pseudopregnant rat ovaries and used as antigen for the development of a monoclonal antibody by the hybridoma technique. Spleen cells of BALB/c mice immunized with purified 20-α-HSD were fused with SP2/0 mouse myeloma cells. Among the colonies of hybrid cells, one (designated mAb-HSD 11) was found to be secreting antibodies (IgM) able to inhibit 20-α-HSD activity. The antibody-secreting hybridome was amplified by ascitic fluid production and the monoclonal antibody purified by Bakerbond ABx procedure. Purified mAb-HSD 11 was able to inhibit 20-α-HSD activity in a dose-dependent manner. Studies of Michaelis constants of 20-α-HSD indicate that this monoclonal antibody increases the K m for 20-α-dihydroprogesterone and decreases the V max.
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