Binding of the complement intermediate C56 to zymosan in acute phase human sera

C56 is known to appear in the fluid phase when zymosan is incubated at 37 degrees C with certain acute phase 'reactor' sera. In the present study, C56 was detected bound to the zymosan particle prior to its appearance free in solution. In reactor sera C56 was formed and released with kinetics similar to that of the generation and decay of a C56-binding site formed when zymosan was incubated with normal serum. Bound and fluid phase C56 was detected only in reactor sera, and was generated only by agents known preferentially to activate the properdin pathway. Elution of C56 from zymosan in hypertonic salt solutions proved to be a convenient step in the partial purification of large amounts of this haemolytically active bimolecular complex.