We have recently reported the isolation from rabbit alveolar macrophages of a receptor which retained its ligand-binding activity for the third component of complement (C3) and for its major proteolytic derived activation fragment (C3b). The isolated receptor demonstrated a greater ability to bind C3b than an equimolar amount of C3. C3b differs from C3 in at least two ways: it is a proteolytic cleavage product of C3 and it lacks the internal thiolester bond of C3. We have analyzed the binding ability of isolated receptor to various C3 and C3b analogs and we demonstrate that the specificity of the C3b-C3b receptor interaction depends upon the lysis of the C3 thiolester bond and accompanying conformational change rather than upon proteolytic cleavage of the C3 molecule. Minimal, if any, binding of C3 with an intact thiolester bond to the isolated receptor was demonstrable.
|Number of pages||3|
|Journal||Journal of Biological Chemistry|
|State||Published - 1982|