The immunoelectrophoretic pattern of properdin in fresh and aged human serum.

Abstract

SummaryWe have described for the first time a technique for demonstrating human properdin in whole serum by immunoelectrophoresis. Utilizing this method, we have noted a change in the immunoelectrophoretic migration of properdin by incubating serum at 37°. There was a concomitant decrease in the functional activity of properdin and CH50, as well as conversion of β1C to a β1A pattern on immunoelectrophoresis. It is probable that the changes in the electrophoretic mobility of properdin resulted from a fundamental change in the properdin molecule.The authors wish to acknowledge the expert technical assistance of Kay Townsend.