Purification of Prophenoloxidase in the Haemolymph ofCalliphora vicina(R. & D.)
- 1 January 1979
- journal article
- research article
- Published by Taylor & Francis in Archives Internationales de Physiologie et de Biochimie
- Vol. 87 (4) , 687-695
- https://doi.org/10.3109/13813457909070529
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.This publication has 14 references indexed in Scilit:
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