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Size separation of sodium dodecyl sulfate complexes of human plasma proteins by capillary electrophoresis employing linear polyacrylamide as a sieving polymer
Author(s) -
Manabe Takashi,
Oota Hideto,
Mukai Jun
Publication year - 1998
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.1150191310
Subject(s) - sodium dodecyl sulfate , chromatography , capillary electrophoresis , chemistry , polyacrylamide , sodium , linear polymer , human plasma , polymer , electrophoresis , gel electrophoresis , polyacrylamide gel electrophoresis , analytical chemistry (journal) , polymer chemistry , biochemistry , organic chemistry , enzyme
Electrophoretic conditions to separate sodium dodecyl sulfate (SDS) complexes of human plasma proteins according to their size differences, by capillary electrophoresis employing linear polyacrylamide as a sieving matrix (LPA‐CE), have been examined. Using the optimized separation conditions, SDS complexes of human plasma proteins not treated with reducing agents were separated into about 40 peaks and shoulders within 60 min. The molecular mass values of major peaks in a separation pattern were estimated from a plot of molecular mass and migration time for standard proteins and some of the major plasma proteins have been identified on the pattern. The electrophoretic conditions were successfully applied for the analysis of proteins in immunoglo‐bulin G (IgG) myeloma sera.