Interaction of C1-inhibitor with the C1r and C1s subcomponents in human C1.
Biochim Biophys Acta
; 576(1): 151-62, 1979 Jan 25.
Article
em En
| MEDLINE
| ID: mdl-760802
ABSTRACT
1. Insoluble IgG-ovalbumin aggregates were used to bind and activate C1 from human serum. The bound C1 provided a useful reagent for studying the interaction of C1 subcomponents with C1-inhibitor. 2. C1-inhibitor bound to both subcomponents (C1r and C1s in C1 and formed stable complexes of respective apparent molecular weights 197,000 and 185,000, as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The binding reaction proceeded more readily with C1s than with C1r and was correlated with the inhibition of C1s esterase activity. 3. At physiological ionic strength, binding of C1-inhibitor to subcomponents C1r and C1s caused release of these subcomponents from the C1-immune aggregates complex, indicating that C1-inhibitor binding decreased the inter-subcomponent binding forces in C1. At low ionic strength, however, this release did not occur.
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Base de dados:
MEDLINE
Assunto principal:
Complemento C1
/
Proteínas Inativadoras do Complemento 1
Limite:
Humans
Idioma:
En
Ano de publicação:
1979
Tipo de documento:
Article