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Amino acid sequence of the trypsin-generated C3d fragment from human complement factor C3
The Biochemical Journal
|September 1, 1985
Summary
Researchers determined the primary structure of human complement C3d (try-C3d) by sequencing peptides. This study reveals 90% of the try-C3d sequence and its homology with human C4B.
Area of Science:
- Biochemistry
- Immunology
- Proteomics
Background:
- Human complement component 3 (C3) plays a critical role in the immune system.
- Understanding the structure of C3d, a fragment of C3, is essential for elucidating its function.
Purpose of the Study:
- To determine the primary amino acid sequence of human C3d (try-C3d).
- To identify sequence homologies with other complement proteins.
Main Methods:
- Peptide fragmentation of try-C3d using CNBr.
- Separation of peptides using high-performance liquid chromatography (HPLC).
- Amino acid sequencing via automatic Edman degradation and enzymatic digestion.
Main Results:
- Complete sequences of five peptides and partial sequences of three peptides were determined.
- 90% of the try-C3d primary structure was elucidated.
- Extensive sequence homology was found between try-C3d and human C4B in their N-terminal regions.
Conclusions:
- The study provides significant insights into the primary structure of human C3d.
- Identified sequence homology suggests evolutionary or functional relationships within the complement system.