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

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

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Transfer is accomplished through activation of metastable binding sites which are transiently revealed by the respective activating enzymes. Cleavage of a critical peptide bond leads to dissociation or dislocation of the activation fragment of a given component and to exposure of structures that are concealed in the native molecule. Owing to the metastable binding site, a molecule can bind to a suitable acceptor and establish firm association with it. Failing collision with the acceptor within a finite time period after activation, the site decays and the molecule remains unbound in the fluid phase.

Regulation Regulation of the positive feedback, and thereby of the entire alternative pathway, is provided by four known mechanisms: spontaneous decay of the metastable binding site of activated C3b, degradation of target-bound C3b, spontaneous decay of the C3/C5 convertase and active disassembly of this enzyme. P1H binds to C3b, and this binding is competitive with that of B or Bb. , 1979a). With the formation of inactive C3b (C3bi),P1H is released and both control proteins are free to attack the next molecule of enzyme or of C3b.

It has now become apparent that in the virus-infected cell model activation of the alternative pathway and cell lysis have different requirements. Activation was manifested by progressive specific uptake of radiolabeled C 3 onto the cell surface. The rate of C 3 uptake was the same in the presence and the absence of properdin. However, properdin did increase the rate of C 3 uptake when antiviral IgG was bound to the cell surface. , 1979). It appears likely that antibody and properdin, which increase the rate of C 3 uptake by the virus-infected cells, also increase the rate of MAC accumulation on the cells.

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