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Nephritic factor: its structure and function and its relationship to initiating factor of the alternative pathway
Scandinavian Journal of Immunology
|January 1, 1976
Summary
Nephritic factor (NF) stabilizes the complement system's C3 convertase enzyme. This protein remains active after dissociation, indicating multiple binding sites for its function in immune responses.
Area of Science:
- Immunology
- Biochemistry
Background:
- Nephritic factor (NF) is a key component in the complement system.
- Understanding NF's structure and function is crucial for immune research.
Purpose of the Study:
- To elucidate the molecular characteristics and functional mechanisms of Nephritic Factor (NF).
- To investigate how NF interacts with and stabilizes complement enzyme complexes.
Main Methods:
- Biochemical analysis of NF's molecular weight and subunit composition.
- Assays to determine NF's role in the assembly and stabilization of C3 convertase.
- Investigation of NF's binding properties and resistance to inhibitors.
Main Results:
- NF has a molecular weight of 170,000 daltons, comprising two disulfide-linked 85,000-dalton chains.
- NF incorporates into fluid-phase C3 convertase and stabilizes cell-bound C3/C5 convertase (EC3b,B).
- Released NF retains binding and stabilizing activity, suggesting multiple binding sites, and is resistant to diisopropylfluorophosphate.
Conclusions:
- Nephritic Factor (NF) is essential for stabilizing complement convertase enzymes.
- NF's ability to remain active after dissociation highlights its significant role in complement regulation.
- The presence of multiple binding sites is inferred from NF's agglutination activity.