Catalase and superoxide dismutase double staining zymogram technique for Deinococcus and Kocuria species exposed to multiple stresses

Superoxide dismutase (SOD) and catalase expression is associated with oxidative stress. Existing techniques for the individual staining of SOD and catalase have been described in the past. The objective of this study was to achieve a simple and rapid technique for the double staining of bacterial SO...

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Bibliographic Details
Published in:Journal of basic microbiology 2009-11, Vol.49 (6), p.593-597
Main Authors: Shukla, Manish R, Yadav, Radhika, Desai, Anjana
Format: Article
Language:English
Subjects:
Catalase
Catalase - metabolism
Deinococcus
Deinococcus - enzymology
Deinococcus radiodurans
Desiccation
Electrophoresis, Polyacrylamide Gel - methods
Enzymes
Ferricyanide
Ferricyanides - metabolism
gamma Radiation
Micrococcaceae - enzymology
Nitroblue Tetrazolium
Oxidative Stress
Precipitation
Protein Isoforms - metabolism
Radiation
Staining and Labeling - methods
Stress
Superoxide dismutase
Superoxide Dismutase - metabolism
Zymogram
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Summary:Superoxide dismutase (SOD) and catalase expression is associated with oxidative stress. Existing techniques for the individual staining of SOD and catalase have been described in the past. The objective of this study was to achieve a simple and rapid technique for the double staining of bacterial SOD and catalase on the same polyacrylamide gel. SOD detection was carried out using nitro-blue tetrazolium (NBT) dye reduction followed by ferricyanide precipitation for negative staining of the catalase enzyme on the same gel. The staining procedure resulted in pale blue SOD bands while catalase appeared as yellow bands against a greenish blue background on the same gel. This technique was used to detect changes in the polymorphic forms of these enzymes in Deinococcus radiodurans R1 and Kocuria sp. C2 subjected to stresses like UV and gamma radiation and desiccation. (© 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)
ISSN:0233-111X
1521-4028
DOI:10.1002/jobm.200900037