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Isolation of Alternative Pathway C3 Convertases Formed in the Presence of C3 Nephritic Factor (C3NeF)

Harvard Medical School at the Robert B. Brigham Hospital, Boston, Mass. 02120

Abstract

Interaction of C3b or EAC43, an erythrocyte intermediate bearing C3b, with B and results in formation of a labile fluid phase or cell-bound alternative pathway C3-convertase,
. C3NeF, purified free of antigenic and functional activated properdin, stabilizes the labile convertase site on EAC43B and thus its capacity to stabilize and permit isolation of fluid phase C3B was examined.

Reaction mixtures containing 3.40 µg ¹³¹I-C3 (C3*) or 1.86 µg ¹²⁵I-B (B*) alone, C3* and B*, C3*, B* and 5 ng , and C3*, B*, and 0.1 units C3NeF in 100 µ1 DGVB⁺⁺ were incubated for 30 min at 30°C, assessed for residual C3* and B* hemolytic activities, and 75 µl subjected to sucrose density ultracentrifugation (UCF). Interaction of C3* and B* did not diminish their hemolytic activities or alter UCF-characteristics. The presence of resulted in 76% depletion of B* and C3* hemolytic activities, but no convertase activity was recognized in the UCF fractions and B* and C3* sedimented at 5.9 S and 8.2 S, respectively.