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Abstract
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 °C and maximum conversion into active state was found between 40 and 50 °C.