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Detection of gelatinolytic enzyme activities after sodium dodecyl sulfate‐electrophoresis and protein blotting
Author(s) -
Moos Jiri
Publication year - 1991
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150120613
Subject(s) - sodium dodecyl sulfate , proteases , nitrocellulose , gel electrophoresis , chemistry , blot , biochemistry , enzyme , chromatography , alkaline lysis , sodium , electrophoresis , proteolytic enzymes , membrane , dna vaccination , organic chemistry , gene , recombinant dna
Visualization of proteases with gelatinolytic activity in sodium dodecyl sulfate gels is described. After conventional sodium dodecyl sulfate‐polycrylamide gel electrophoresis, proteins are transferred onto nitrocellulose membranes preincubated with 0.3% gelatine. During the protein electrotransfer, the proteases are renaturated and their enzymatic activity is restored. After nonspecific protein staining, bands with proteolytic activity appear as white areas on a dark background.