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Capillary electrophoretic resolution of phosphorylated peptide isomers using micellar solutions and coated capillaries
Author(s) -
Tadey Tanya,
Purdy William C.
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150160193
Subject(s) - capillary electrophoresis , sodium dodecyl sulfate , micelle , chemistry , selectivity , chromatography , resolution (logic) , peptide , capillary action , electrophoresis , micellar electrokinetic chromatography , phosphate , analytical chemistry (journal) , materials science , organic chemistry , biochemistry , aqueous solution , catalysis , artificial intelligence , computer science , composite material
The addition of sodium dodecyl sulfate (SDS) micelles in the running buffer can be used to resolve mono‐ and diphosphorylated isomers of the insulin receptor peptide by capillary electrophoresis. The effect of SDS on peptide resolution is very dependent on pH. Complete resolution of three monophosphorylated isomers is achieved in uncoated capillaries filled with phosphate buffer containing 25 m M SDS and buffered at pH 6.1. Resolution of the diphosphorylated isomers can be significantly improved by using polyacryla‐mide coated capillaries. In coated capillaries electroosmotic flow is negligible and the migration order of the isomers is reversed. This allows for a longer period of interaction between the diphosphorylated isomers and the micelle and therefore selectivity is improved. Efficiency of all peptide isomers was also improved in coated capillaries due to reduced adsorption to the capillary wall.