Specific indication of hemoproteins in polyacrylamide gels using a double-staining process |
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Authors: | R T Francis R R Becker |
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Affiliation: | Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331 USA |
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Abstract: | Hemoproteins were revealed in polyacrylamide gels in the presence of sodium dodecyl sulfate by staining with different benzidine derivatives. When the protein samples were treated with either beta-mercaptoethanol or dithiothreitol, a significant decrease in peroxidase activity of the proteins possessing noncovalently bound heme led to diminished staining. However, when Coomassie blue R-250 staining followed the hemespecific stain it was observed that the hemoprotein bands stained more intensely than duplicate sample bands that had been stained only with the Coomassie blue R-250. This staining property allows the indication of hemoproteins in gels even after the peroxidase yield has been significantly depleted by reducing agents. |
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Keywords: | Hemoproteins peroxidase activity tetramethylbenzidine diaminobenzidine dimethoxybenzidine staining |
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