Direct determination of the redox status of cysteine residues in proteins in vivo
| Autor: | Hara, Satoshi, Tatenaka, Y., Ohuchi, Y., HISABORI, TORU |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Ultraviolet Rays
Blotting Western Arabidopsis Biophysics Biochemistry Redox RoGFP Maleimides chemistry.chemical_compound Escherichia coli Humans Moiety Electrophoresis Gel Two-Dimensional Cysteine Sulfhydryl Compounds Molecular Biology Maleimide Glyceraldehyde 3-phosphate dehydrogenase chemistry.chemical_classification biology Proteins DNA Cell Biology Oxidative Stress chemistry Thiol biology.protein Oxidation-Reduction HeLa Cells |
| Zdroj: | Biochemical and Biophysical Research Communications. 456:339-343 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2014.11.082 |
| Popis: | The redox states of proteins in cells are key factors in many cellular processes. To determine the redox status of cysteinyl thiol groups in proteins in vivo, we developed a new maleimide reagent, a photocleavable maleimide-conjugated single stranded DNA (DNA-PCMal). The DNA moiety of DNA-PCMal is easily removed by UV-irradiation, allowing DNA-PCMal to be used in Western blotting applications. Thereby the state of thiol groups in intracellular proteins can be directly evaluated. This new maleimide compound can provide information concerning redox proteins in vivo, which is important for our understanding of redox networks in the cell. |
| Databáze: | OpenAIRE |
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