Electrophoresis of Phosphoproteins on a Tandem Polymerized Gel
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Le résumé fourni par la source
A substrate with n phosphorylated sites may have 2 n phosphor-forms for temporal-spatial regulation of biological events. Because phosphates do not significantly change molecular masses but net charges of proteins, those isoforms cannot be separated by regular mass-based sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE). A tandem polymerized gel was developed to resolve phosphor-isoforms with different masses, charges, and posttranslational modifications. Without the usage of SDS, the electrophoresis was primarily performed on three adjacent acidic polyacrylamide gels. After being concentrated on a stacking gel, protonated proteins were then separated on the Zr 4+ immobilized gel through the coordination of metal ions with phosphates followed by further charge and mass ( z/m )-based electrophoretic separation on a TiO 2 containing gel. The presence of TiO 2 nanoparticles in the third gel is aimed for the initiation of the polymerization of acrylamide in acidic conditions upon ultraviolet irradiation. Distinct isoforms of α-S1-casein, α-S2-casein, β-casein, and κ casein model proteins located on 11, 8, 8, and 7 different bands of the tandem gel were unambiguously identified, respectively. With the tandem polymerized gel electrophoresis, new phosphorylation events that may occur simultaneously or sequentially were discovered in not only model proteins but also complex biological samples including human saliva, chicken egg, and sprouting maize. This provides a new tool to dissect complex biological processes that are triggered by dynamic phosphorylation events.
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Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- Electrophoresis of Phosphoproteins on a Tandem Polymerized Gel
- Date Crossref
- 10/05/2022
- Éditeur
- American Chemical Society (ACS)
- Type
- journal-article
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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Central China Normal University pays non établi dans la noticeUniversité ou école supérieure
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Guangdong Academy of Agricultural Sciences pays non établi dans la noticeOrganisme public
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Guangxi University pays non établi dans la noticeUniversité ou école supérieure
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Guangdong Key Laboratory for Crop Germplasm Resources Prevention and Utilization pays non établi dans la noticeStructure de recherche
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College of Chemistry Laboratory of Mass Spectrometry pays non établi dans la noticeUniversité ou école supérieure
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College of Life Science and Technology Center for Instrumental Analysis pays non établi dans la noticeUniversité ou école supérieure
Central China Normal University, Guangdong Academy of Agricultural Sciences et Guangxi University, avec 3 autres affiliations.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.