By Gordon D. Ross
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Young, J. Immunol. 132, 3019-3027 (1984). 27. M. A. Kerr and J. Gagnon, Biochem. J. 205, 59-67 (1982). 28. W. Opferkuch, H. J. Rapp, H. R. Colten, and T. Borsos, J. Immunol. 106, 407-413 (1971). 29. N. R. Cooper and H. J. Müller-Eberhard, J. Exp. Med. 132, 775-793 (1970). 30. M. A. Kerr, Biochem. J. 183, 615-622 (1979). 31. M. R. Mardiney, H. J. Müller-Eberhard, and J. D. Feldman, Am. J. Pathol. 53, 253-262 (1968). 32. H. J. Müller-Eberhard, A. P. Dalmasso, and M. A. Calcott, J. Exp. Med. 123, 33-54 (1966).
Nati. Acad. Sci. 77, 7014 (1980). 1. The Classical Pathway 29 membranes takes place within 10 to 20 sec, but activation is a much slower process. , antibody-coated red cells), activation takes 3-20 min to come to comple tion (8-10). This relatively slow rate of activation should be explained if only a small proportion of the Cl binding sites were capable of activating Cl. The reaction of Cl with target surfaces is known to be a dynamic process with continuous association and dissociation. It is therefore pos sible that Cl molecules attached at nonactivating sites successively disso ciate and reassociate until they bind to a site where activation can take place.
C3(H20),Bb is the first enzyme of the pathway capable of forming metastable C3b. The enzyme itself is confined to the fluid phase, but metastable C3b can diffuse up to 300 A to find and attach to nearby particles. Note that the process does not rely on initiators or activating particles but is spontaneous. 54 Michael K. Pangburn Fig. 5. Time course of C3b deposition on alternative pathway activators. Rabbit erythrocytes (ER), zymosan (yeast cell walls), and E. coli strain 04 were incubated at 37°C with human serum depleted of complement component C7 and containing C3 radiolabeled with 125 I.