Abstract
Upon activation of the third component of complement (C3) by the classical or alternative pathway convertases, an opsonically active form of C3 gets firmly bound to a wide variety of surfaces. To analyze the forms of solid phase C3, dextran gel beads (675,superfine) were incubated with normal human serum in veronal-buffered saline 5 mM Mg++, 10 mM ethylene glycol tetraacetic acid (EGTA) for timed intervals, and samples washed with phosphate-buffered saline (200 × volume) at room temperature. Gel beads were solubilized with Dextranase, and solutions analyzed on sodium dodecyl sulfate gels in unreduced and reduced (2-Mercaptoethanol) form. C3 fragments accounted for more than 90% of the total proteins present. A 175,000 M.W. fragment was the predominant species at 5′, 10′, 15′, 20′ and 30 minute intervals, and was maximum at 15′. Other fragments were detected as early as 5′ (155,000 M.W.), 10′ (138,000 and 23,000), 15′ (110,000), and at 60′ only these and not the 175,000 M.W. fragment were detected. Solubilization of dextran gel beads with Dextranase appears to be an ideal vehicle for the analysis of solid phase activation and degradation of C3 and the relationship of the deposited fragments to these various biological activities including opsonization and immune adherence. Supported by U.S.P.H.S. Research Grant AM 16392.
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