Abstract
It has been shown previously that methylamine is incorporated into the alpha-chain of human C4, resulting in a loss of haemolytic function and the appearance of a free thiol group in the molecule. In the present study it was demonstrated that a fragment resembling C4d is liberated from C4 by trypsin. The fragment--Try-C4d--contains both the methylamine binding site and the free thiol group. When separated on DEAE-Sepharose, four types of Try-C4d, differing in charge and size, could be defined. The size difference was found to parallel the presence of Chido and Rodgers blood group antigens. Fragments of Mr 30,000 carried the Rodgers antigen and the Chido antigen was expressed on fragments of Mr 28,000.
Original language | English |
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Pages (from-to) | 1655-65 |
Journal | Mol Immunol |
Volume | 19 |
Issue number | 2 |
Publication status | Published - 1982 |
Externally published | Yes |
Bibliographical note
12Subject classification (UKÄ)
- Medicinal Chemistry
Free keywords
- Isoantigens/*analysis
- Humans
- Electrophoresis
- Polyacrylamide Gel
- Complement C4/*immunology/isolation & purification/metabolism
- Gel
- DEAE-Cellulose
- Chromatography
- Amino Acid Sequence
- Amino Acids/analysis
- Methylamines/metabolism
- Molecular Weight
- Peptide Fragments/*immunology/isolation & purification
- Research Support
- Non-U.S. Gov't
- Sulfhydryl Compounds/metabolism
- Trypsin