Separation and identification of four distinct serine-phosphorylation states of ovalbumin by Phos-tag affinity electrophoresis |
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Authors: | Kinoshita-Kikuta Emiko Kinoshita Eiji Koike Tohru |
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Institution: | Department of Functional Molecular Science, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan. |
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Abstract: | Ovalbumin (OVA) derived from egg white contains two residues that can be phosphorylated: Ser-68 and Ser-344. Native polyacrylamide gel electrophoresis(PAGE) shows the presence of three distinct migration bands corresponding to phosphorylation states with two, one, or no phosphate groups, respectively. Phosphate-affinity sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE; Zn(2+)-Phos-tag SDS-PAGE), on the other hand, showed the presence of four distinct phosphorylated states in intact OVA. In addition to the diphosphorylated and nonphosphorylated forms, two distinct species, one with a phosphate group at Ser-68 and one with a phosphate group at Ser-344, were separately visualized. The content of the OVA monophosphorylated at Ser-68 was greater than that of OVA monophosphorylated at Ser-344. Zn(2+)-Phos-tag SDS-PAGE is therefore a useful method for the quantitative analysis of the detailed phosphorylation status of food proteins. |
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Keywords: | Affinity electrophoresis Ovalbumin Phosphorylation Phos‐tag |
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