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Polymerization of human transcortin in plasma
Journal of Steroid Biochemistry
|June 1, 1984
Summary
Polymers of native transcortin were found in plasma and purified samples. These transcortin polymers are reversible upon dilution and can be disaggregated by specific agents, but not cortisol.
Area of Science:
- Biochemistry
- Immunology
Background:
- Transcortin is a key protein in corticosteroid transport.
- Understanding transcortin's behavior in plasma is crucial for corticosteroid regulation studies.
Purpose of the Study:
- To identify and characterize polymers of native transcortin in plasma.
- To investigate the reversibility and disaggregation of transcortin polymers.
Main Methods:
- Radial immunodiffusion using antiserum against purified transcortin.
- Spectrophotometric scans to monitor polymerization kinetics.
- Testing disaggregation agents like sodium dodecyl sulphate and dithiothreitol.
Main Results:
- Polymers of native transcortin were identified in plasma via precipitin bands.
- Polymer size diminished upon dilution, indicating reversibility.
- Purified transcortin also showed dilution-reversible polymerization.
- Sodium dodecyl sulphate and dithiothreitol induced disaggregation, but cortisol did not.
Conclusions:
- Native transcortin can form reversible polymers in plasma.
- The polymerization process is influenced by dilution and specific chemical agents.
- Cortisol does not appear to directly disaggregate transcortin polymers.