Purification of prophenoloxidase in the haemolymph of Calliphora vicina (R. & D.).

An improved method for the purification of prophenoloxidase is described. The proenzyme was purified 400 fold in homogenous form. The purity was tested by disc-electrophoresis and the molecular weight was found to be 87 000 in comparison to the mobility of marker enzymes, which were run simultaneously in SDS-gel electrophoresis. The proenzyme was denatured at 80 degrees C and maximum conversion into active state was found between 40 and 50 degrees C.