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The Journal of Immunology, 1976, 116: 1729.
Copyright © 1976 by The American Association of Immunologists, Inc.

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The Role of Factor D for the Interaction of Zymosan with Components of the Properdin System: Studies with D-Depleted Guinea Pig Serum

V. Brade, R. Burger, D. Bitter-Suermann and U. Hadding

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 D 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 D, 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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