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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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
1996
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| In: |
Fett
Year: 1996, Volume: 98, Issue: 5, Pages: 183-184 |
| ISSN: | 1521-4133 |
| DOI: | 10.1002/lipi.19960980507 |
| Online Access: | Verlag, kostenfrei, Volltext: https://doi.org/10.1002/lipi.19960980507 Verlag, kostenfrei, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/lipi.19960980507 
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| Author Notes: | O. Heinisch, E. Kowalski, H. Ludwig and B. Tauscher, Karlsruhe (Germany) |
| Summary: | 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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| Item Description: | Gesehen am 12.02.2026 |
| Physical Description: | Online Resource |
| ISSN: | 1521-4133 |
| DOI: | 10.1002/lipi.19960980507 |