ovalbumin and 1-3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol

ovalbumin has been researched along with 1-3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol* in 1 studies

Other Studies

1 other study(ies) available for ovalbumin and 1-3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol

Article	Year
Separation and identification of four distinct serine-phosphorylation states of ovalbumin by Phos-tag affinity electrophoresis. Electrophoresis, 2012, Volume: 33, Issue:5 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. Topics: Amino Acid Sequence; Animals; Chickens; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Mass Spectrometry; Molecular Sequence Data; Ovalbumin; Phosphoproteins; Phosphorylation; Pyridines; Serine	2012

Article

Year

Separation and identification of four distinct serine-phosphorylation states of ovalbumin by Phos-tag affinity electrophoresis.

Electrophoresis, 2012, Volume: 33, Issue:5

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.

Topics: Amino Acid Sequence; Animals; Chickens; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Mass Spectrometry; Molecular Sequence Data; Ovalbumin; Phosphoproteins; Phosphorylation; Pyridines; Serine

2012