Download Advances in Immunology, Vol. 29 by Henry G. Kunkel and Frank J. Dixon (Eds.) PDF

By Henry G. Kunkel and Frank J. Dixon (Eds.)

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The functional half-life of the C3b was 18 minutes. 6 minutes. , 1978). It was this experiment that suggested a recognition function for C3b but provided no information on whether or not the metastable binding site of C3b was responsible for this function. The results apparently ruled out P l H and C3bINA as recognition proteins because they failed to protect autologous cells from attack. Second, C3b bound to sheep erythrocytes, which is susceptible to control, became resistant to control upon removal of cell surface sialic acid (Fearon, 1978; Pangburn and Muller-Eberhard, 1978a).

The function of C3b in phagocytosis has not been completely elucidated. , 1968). , 1980). , 1980). Peritoneal macrophages could be converted in vitro from cells mediating only attachment to cells promoting both attachment and ingestion of C3b-coated particles. Conversion required treatment of the cells with supernatants of cultures containing T lymphocytes and triggered macrophages (Griffin and Griffin, 1979). The role of C3bi-C3bi receptor interaction in phagocytosis remains to be investigated.

1979). , 1979) or to the PROTEINSOF THE Molecular TABLE VIII MEMBRANE ATTACK PATHWAY OF COMPLEMENT Protein weight No. of chains c5 C6 c7 C8 c9 180,000 128,000 121,000 154,000 72,000 2 1 1 3 1 Electrophoretic mobility PI P2 P2 Y1 CY Serum conc. (CLdml) 70 60 55 55 60 31 ALTERNATIVE PATHWAY OF COMPLEMENT "J . 9. Assembly of an intact cytolytic alternative pathway from eleven purified proteins of human serum. Reaction mixtures (each 160 pl) containing 10' erythrocytes, MgGVB, and various amounts of either C4-depleted serum or the isolated component mixture were incubated for 10 minutes at 37°C.

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