-transparent.png){kind=logo}
The interaction of C1 inhibitor with complement component C1 bound to immune complexes was examined by using 125I-labelled C1 subcomponents. The inhibitor binds rapidly to subcomponent C1s, and more slowly to subcomponent C1r. Formation of the C1r-C1 inhibitor complex causes rapid dissociation of subcomponents C1r and C1s from the antibody-antigen-component C1 aggregate. The rate and extent of this release are proportional to C1 Inhibitor concentration and are also dependent on ionic strength. Results obtained with purified C1 Inhibitor, plasma or serum as source of C1 Inhibitor are all closely comparable. Only slight dissociation of subcomponent C1q is observed under the same range of conditions. The implications of the release phenomenon are discussed in relation to the structure of component C1 and the possibility of differential turnover of C1 subcomponents.
R B Sim, and
G J Arlaud, and
M G Colomb
April 1984,
European journal of biochemistry,
R B Sim, and
G J Arlaud, and
M G Colomb
February 2003,
Planta medica,
R B Sim, and
G J Arlaud, and
M G Colomb
July 1989,
Clinical and experimental immunology,
R B Sim, and
G J Arlaud, and
M G Colomb
February 1991,
Immunological investigations,
R B Sim, and
G J Arlaud, and
M G Colomb
January 1981,
Methods in enzymology,
R B Sim, and
G J Arlaud, and
M G Colomb
May 1991,
Clinical and experimental immunology,
R B Sim, and
G J Arlaud, and
M G Colomb
November 1983,
Clinical and experimental immunology,
R B Sim, and
G J Arlaud, and
M G Colomb
August 2000,
Transplantation proceedings,
R B Sim, and
G J Arlaud, and
M G Colomb
May 1978,
Immunochemistry,
R B Sim, and
G J Arlaud, and
M G Colomb
February 2018,
Immunobiology,
