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Institut für Medizinische Mikrobiologie der Universität Mainz, Germany
Abstract
Serum was depleted of factor D by gel filtration and immunoabsorption with unsolubilized anti-D IgG. Substitution of this reagent (RD) with purified
was found to fully reconstitute its function. In the following experiments the reaction of zymosan (Z) with RD was investigated; therefore these studies are concerned with the role of Factor D for the interaction of Z with components of the properdin system.
RD was incubated for 30 min at 0°C, or for 30 min at 37°C, with Z (10 mg/ml) in the presence of EGTA. After centrifugation both supernatants, as well as the corresponding Z particles, were analyzed. Both supernatants were found to contain identical amounts of B, whereas C3 was slightly reduced in the 37°C supernatant. After addition of Z and of purified
, both supernatants supported the formation of the C3-cleaving ZX-complex with the same efficiency as untreated RD. Thus, incubation of Z with RD was only followed by a slight loss of C3; no other factors of the properdin system appeared to be reduced in their activity.
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