3,3′,5,5′-Tetramethylbenzidine/H2O2 staining is not specific for heme proteins separated by gel electrophoresis |
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| Authors: | David J Miller D J D Nicholas |
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| Institution: | Department of Agricultural Biochemistry, Waite Agricultural Research Institute, University of Adelaide, Glen Osmond, South Australia 5064, Australia |
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| Abstract: | Staining of sodium dodecyl sulfate or lithium dodecyl sulfate gels with 3,3',5,5'-tetramethylbenzidine (TMBZ)/H2O2 after electrophoresis has frequently been used as a specific method of detecting heme proteins. That TMBZ is an electron donor for O2 reduction by the nonheme-soluble cytochrome oxidase/nitrite reductase from Nitrosomonas europaea is now shown; this protein is detected by the TMBZ/H2O2 method. A method for the determination of TMBZ oxidase activity is given; hence, the detection of artifactual staining due to proteins of this type is possible. |
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| Keywords: | heme staining oxidases copper proteins nitrite reductases Nitrosomonas europaea nitrifying bacteria |
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