Labeling and quantifying sites of protein palmitoylation
As a reversible posttranslational modification, protein palmitoylation has the potential to regulate the trafficking and function of a variety of proteins. However, the extent, function, and dynamic nature of palmitoylation are poorly resolved because of limitations in assay methods. Here, we introd...
| Veröffentlicht in: | BioTechniques. - 1993. - 36(2004), 2 vom: 26. Feb., Seite 276-85 |
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| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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| Zugriff auf das übergeordnete Werk: | BioTechniques |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Membrane Proteins Nerve Tissue Proteins Palmitates Proteins SNAP25 protein, human Snap25 protein, mouse Synaptosomal-Associated Protein 25 mehr... |
| Zusammenfassung: | As a reversible posttranslational modification, protein palmitoylation has the potential to regulate the trafficking and function of a variety of proteins. However, the extent, function, and dynamic nature of palmitoylation are poorly resolved because of limitations in assay methods. Here, we introduce methods where hydroxylamine-mediated cleavage of the palmitoyl-thioester bond generates a free sulfhydryl, which can then be specifically labeled with sulfhydryl-reactive reagents. This methodology is more sensitive and allows for quantitative estimates of palmitoylation. Unlike other techniques used to assay posttranslational modifications, the techniques we have developed can label all sites of modification with a variety of probes, radiolabeled or nonradioactive, and can be used to assay the palmitoylation of proteins expressed in vivo in brain or other tissues |
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| Beschreibung: | Date Completed 16.09.2004 Date Revised 07.06.2018 published: Print Citation Status MEDLINE |
| ISSN: | 0736-6205 |