Structural, immunological and functional comparisons of factor H, rheumatoid arthritis protein (RHP), and its apparent normal counterpart (N-RHP)
| Autor: | Peter Weber, Carmen L. Rosano, Hurwitz C, Karim E. Hechemy, Nourollah Parhami |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Antigenicity
Glycosylation Complement Activating Enzymes Immunology chemical and pharmacologic phenomena chemistry.chemical_compound Epitopes Animals Humans Bovine serum albumin Amino Acids Molecular Biology chemistry.chemical_classification biology Isoelectric focusing Blood Proteins Complement System Proteins Precipitin Blood proteins Complement system Amino acid chemistry Biochemistry Complement Factor H biology.protein Rabbits |
| Zdroj: | Molecular immunology. 32(16) |
| ISSN: | 0161-5890 |
| Popis: | The isolation and characterization of two human serum proteins, RHP and N-RHP, are described. N-RHP appears to be the normal counterpart of RHP which is found at elevated levels in sera of patients with rheumatoid arthritis [Rosano et al. (1988b) Inflammation 12, 351–360]. Although both proteins crossreact with anti-Factor H and have identical N-terminal amino acid sequences, they differ from Factor H in pI, solubility at low ionic strength, and in glycosylation. RHP differs from Factor H and N-RHP in antigenicity in the rabbit, in effect on the C1q-anti-C1q precipitin reaction, and in ability to disaggregate C1, the first component of the complement system. Removal of RHP, N-RHP and Factor H from binding to C1q is a prerequesite for separation of RHP and N-RHP from Factor H by anion exchange chromatography and isoelectric focusing. The finding of uniquely demonstrable RHP activity (enhancement of C1q-anti-C1q precipitin activity) in unfractionated sera from patients with rheumatoid arthritis, but not in normal sera, suggests that RHP is not an artefact of Factor H produced during isolation. |
| Databáze: | OpenAIRE |
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