Purification and some physical properties of a chymotrypsin-like protease of the larva of the hornet, Vespa orientalis

URN to cite this document:: urn:nbn:de:bvb:355-epub-161308
DOI to cite this document:: 10.5283/epub.16130

Jany, Klaus D. ; Pfleiderer, Gerhard ; Molitoris, Hans-Peter

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Date of publication of this fulltext: 27 Sep 2010 11:13

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Abstract

A chymotrypsin-like endopeptidase has been purified by ion-exchange chromatography, affinity chromatography, and gel filtration. The enzyme preparation is homogeneous in the ultracentrifuge and disc electrophoresis. The enzyme is proved to be free from any other proteolytic activities. The molecular weight of the proteinase as determined with several techniques (ultracentrifugation, gel ...