Covalent linkage of C3 to properdin during complement activation.
Eur J Immunol
; 25(5): 1481-4, 1995 May.
Article
em En
| MEDLINE
| ID: mdl-7774654
ABSTRACT
Activation of the alternative complement pathway of serum produces complexes of properdin (P) and C3 as measured in a double antibody enzyme-linked immunosorbent assay. When purified from serum, these complexes decrease factor B hemolytic activity in serum and do not restore the alternative pathway hemolytic activity of serum deficient in P. Sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of activated serum containing biotinylated P, followed by blotting to nitrocellulose and development with streptavidin-alkaline phosphatase revealed a band at 53 kDa for monomeric P and an additional band at 160 kDa. P samples eluted from zymosan and purified from activated serum revealed a band at 116 kDa for C3 alpha and 74 kDa for C3 beta, and an additional band at 160 kDa when analyzed by SDS-PAGE, Western blotting and development with antibody to C3. The appearance of a 160 kDa band containing P and C3 indicates that these proteins are contained in a complex formed during activation of the alternative pathway. Activation of a purified reagent mixture containing factors B, D, and H, and 125I-labeled P or 125I-labeled C3, followed by SDS-PAGE and autoradiography confirmed the presence of a 160-kDa band which disappeared following hydroxylamine treatment of the sample. These data are consistent with a covalent linkage of C3 to P via the C3 alpha chain, producing the 160-kDa complex.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Properdina
/
Complemento C3b
/
Via Alternativa do Complemento
Limite:
Humans
Idioma:
En
Revista:
Eur J Immunol
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Estados Unidos