Staining for soybean lipoxygenase activity in electrophoretic gels

A staining method for lipoxygenase in electrophoretic gels is described which is based on the staining of hydroperoxides, as reaction products of added substrates, by N,N-dimethyl-p-phenylenediamine. Soybean lipoxygenase (EC 1.13.11.12) was detected after gel electrophoresis for anodic proteins unde...

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Hauptverfasser: Heinisch, Oliver (VerfasserIn) , Kowalski, Elisabeth (VerfasserIn) , Ludwig, Horst (VerfasserIn) , Tauscher, Bernhard (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 1996
In: Fett
Year: 1996, Jahrgang: 98, Heft: 5, Pages: 183-184
ISSN:1521-4133
DOI:10.1002/lipi.19960980507
Online-Zugang:Verlag, kostenfrei, Volltext: https://doi.org/10.1002/lipi.19960980507
Verlag, kostenfrei, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/lipi.19960980507
Volltext
Verfasserangaben:O. Heinisch, E. Kowalski, H. Ludwig and B. Tauscher, Karlsruhe (Germany)
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Zusammenfassung:A staining method for lipoxygenase in electrophoretic gels is described which is based on the staining of hydroperoxides, as reaction products of added substrates, by N,N-dimethyl-p-phenylenediamine. Soybean lipoxygenase (EC 1.13.11.12) was detected after gel electrophoresis for anodic proteins under non-denaturating conditions and was compared to soybean lipoxygenase stained by Coomassie Brilliant Blue. Specifity of the method was checked by use of heat-denaturated lipoxygenase, tyrosinase and substrate absence. Staining intensity has been found to be proportional to the enzyme activity.
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Beschreibung:Online Resource
ISSN:1521-4133
DOI:10.1002/lipi.19960980507