Purification and characterization of RHP (factor H) and study of its interactions with the first component of complement.
RHP has been purified from the plasma of both normal individuals and patients with rheumatoid arthritis (RA). RHP from both these sources was shown to be identical with Factor H by reaction with antisera and N-terminal amino acid sequence analysis. Factor H, from both normal and RA sera, inhibited the solubilization of immune precipitates but did not affect prevention of immune precipitation. Factor H was shown to inhibit the haemolytic activity of fluid-phase C1, but unlike C1-inhibitor, it had little effect on C1 bound to EA (EAC1). Factor H was shown to complex with intact C1, to isolated C1q and to the C1r:C1s tetramer. However, binding of factor H to C1 did not dissociate the C1 macromolecule. A C1-Factor H complex was detected in the serum and plasma from normal individuals and patients with systemic lupus erythematosus and RA. Serum levels of this complex were reduced, by EDTA-treatment of serum and by activation of complement by the classical pathway.
Holme
E R
ER
Department of Pathology, University of Glasgow, Western Infirmary, U.K.
Qi
M
M
Ahmed
A E
AE
Veitch
J
J
Auda
G
G
Whaley
K
K
D001172:Arthritis, Rheumatoid / Q000097:blood*; D003172:Complement C1 / Q000502:physiology*; D003174:Complement C1 Inactivator Proteins / Q000494:pharmacology; D003180:Complement C3b Inactivator Proteins / Q000302:isolation & purification / Q000502:physiology*; D017242:Complement Factor H; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding
C493495:CFH protein, human; D003172:Complement C1; D003174:Complement C1 Inactivator Proteins; D003180:Complement C3b Inactivator Proteins; D046911:Macromolecular Substances; D017242:Complement Factor H