Purification of prophenoloxidase in the haemolymph of Calliphora vicina (R. & D.).
作者信息
Naqvi S N, Karlson P
出版信息
Arch Int Physiol Biochim. 1979 Oct;87(4):687-95. doi: 10.3109/13813457909070529.
PMID:93886
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 degrees C and maximum conversion into active state was found between 40 and 50 degrees C.
摘要
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Purification of prophenoloxidase in the haemolymph of Calliphora vicina (R. & D.).
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