Separation of Glutathione Transferase Subunits from Proteus vulgaris by Two-Dimensional Gel Electrophoresis
| Autor: | Cheng-I Chien, Giaming Hong, Yi-Chih Chien |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_classification
Gel electrophoresis Two-dimensional gel electrophoresis biology Molecular mass Protein subunit Proteus vulgaris General Medicine Gel electrophoresis of proteins biology.organism_classification Applied Microbiology and Biotechnology Microbiology Molecular biology Chromatography Affinity Molecular Weight Protein Subunits Enzyme chemistry Affinity chromatography Biochemistry Electrophoresis Gel Two-Dimensional Isoelectric Point Glutathione Transferase |
| Zdroj: | Current Microbiology. 47:352-354 |
| ISSN: | 1432-0991 0343-8651 |
| DOI: | 10.1007/s00284-002-3977-1 |
| Popis: | Cytosolic glutathione transferases of Proteus vulgaris were purified by affinity chromatography and characterized by two-dimensional gel electrophoresis. Four different subunits were identified, and each subunit contained a different molecular mass, ranging from 26.2 kDa to 28.5 kDa; a different pI value, ranging from 8.2 to 9.4; and a different amount of protein fraction, ranging from 10% to 56%. All four subunits existed as basic proteins (pI > 7.0). From these results, we concluded that multiple forms of glutathione transferase enzymes existed in Proteus vulgaris, and four different glutathione transferase subunits were separated by 2-D gel electrophoresis. |
| Databáze: | OpenAIRE |
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