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Monoclonal antibodies to hog thyroglobulin recognizing disulfide-dependent conformational structures
Molecular Immunology
|July 1, 1984
Summary
Monoclonal antibodies (MAbs) targeting hog thyroglobulin (Tg) were developed and classified into three groups based on distinct determinants. These antibodies recognized tryptic fragments, but immunoreactivity was lost upon disulfide bond reduction.
Area of Science:
- Immunology
- Biochemistry
Background:
- Monoclonal antibodies (MAbs) are crucial tools in biological research and diagnostics.
- Thyroglobulin (Tg) is a key protein in thyroid hormone synthesis.
Purpose of the Study:
- To develop and characterize monoclonal antibodies against hog thyroglobulin.
- To investigate the epitope mapping of these MAbs on Tg.
Main Methods:
- Hybridoma technology was used to generate MAbs against hog Tg.
- MAbs were classified based on their reactivity to different determinants.
- Immunoreactivity was assessed after protein reduction and enzymatic digestion.
- Tryptic fragments were analyzed using SDS-PAGE and Western blotting.
Main Results:
- Five MAbs were generated and grouped into three distinct determinant-recognizing categories.
- MAb 16 was IgG2b, while others were IgG1.
- Immunoreactivity was retained after proteolytic digestion but lost after reduction of disulfide bonds.
- Tryptic fragments of varying sizes reacted with MAbs, indicating conserved epitopes.
Conclusions:
- The study successfully generated and characterized MAbs to hog Tg.
- Disulfide bonds are critical for the integrity of the recognized epitopes on Tg.
- These MAbs can be used for further studies on Tg structure and function.