By Henry G. Kunkel and Frank J. Dixon (Eds.)
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Additional resources for Advances in Immunology, Vol. 29
Since factor D, the activating enzyme of factor B, is not consumed in the reaction, a chain reaction is created (Miiller-Eberhard, 1978). b y factor D, its activating enzyme, which results in formation of the C 3 convertase of the alternative pathway, C3b,Bb. , 1974). In acting upon C3, the enzyme supplies in a short period of time many molecules of C3b, each of which is capable of initiating the formation of a molecule of C 3 convertase provided the supply of factor B is not limiting. Factor D, which has no precursor but is always available in active form, is not incorporated into the enzyme complex and can therefore activate many C3b,B complexes (Lesavre and Miiller-Eberhard, 1978).
4. E. This concept is based on the following experimental evidence. First, human C3b was bound to rabbit erythrocytes and the cells were then exposed at 23°C to autologous rabbit P1H and C3bINA. 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.
It is considerably enhanced by treatment of the bound C3b with @1Hand C3bINA. , 1980). An unusual adaptation of a parasite to the effects of complement is exemplified by Babesiu rodhaini (Chapman and Ward, 1977). This protozoan uses the alternative pathway to effect penetration into the erythrocytes of its host, the rat. That the pathway mediates parasitization was shown by its abrogation when sera depleted of C 3 or factor B were used in the test system. It is thought that bound C3b interacts with C3b receptors on the rat erythrocytes, thereby bringing the parasite into proper contact for penetration.
Advances in Immunology, Vol. 29 by Henry G. Kunkel and Frank J. Dixon (Eds.)