Separation and identification of four distinct serine-phosphorylation states of ovalbumin by Phos-tag affinity electrophoresis.
Electrophoresis
; 33(5): 849-55, 2012 Mar.
Article
en En
| MEDLINE
| ID: mdl-22522539
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.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fosfoproteínas
/
Piridinas
/
Serina
/
Ovalbúmina
/
Electroforesis en Gel de Poliacrilamida
Tipo de estudio:
Diagnostic_studies
Límite:
Animals
Idioma:
En
Revista:
Electrophoresis
Año:
2012
Tipo del documento:
Article
País de afiliación:
Japón