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Two‐dimensional electrophoresis of plasma proteins and high density lipoproteins during inflammation
Author(s) -
Choukaife Ala,
Visvikis Sophia,
Steinmetz Josiane,
Galteau MarieMadeleine,
Kabbaj Ouafae,
Férard Georges,
Métais Pierre,
Siest Gérard
Publication year - 1989
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.1150101110
Subject(s) - isoelectric point , chemistry , lipoprotein , isoelectric focusing , apolipoprotein b , gel electrophoresis , apolipoprotein e , sodium dodecyl sulfate , urea , electrophoresis , polyacrylamide gel electrophoresis , chromatography , biochemistry , cholesterol , enzyme , medicine , disease
Plasma protein and lipoprotein fractions of five patients were analyzed on day 1, 5, and 15 after severe head injury by combining three types of two‐dimensional electrophoresis (2‐DE) to obtain information on lipoprotein and apolipoprotein composition. On analysis under nondenaturing conditions in both dimensions on day 5, the samples show modifications of isoelectric point (p I ) and molecular weight ( M r ) properties of the high density lipoprotein (HDL) fraction in addition to an increase in inflammatory proteins and a return to a normal pattern on day 15. In the second type of 2‐DE the samples were analyzed employing isoelectric focusing without denaturant in the first dimension, followed by sodium dodecyl sulfate (SDS) in the second dimension in order to study the protein composition of lipoprotein fractions. On day 5, a decrease of the apolipoproteins apo A‐I, apo A‐II, and apo C were noted, with simultaneous appearance of an unidentified protein with M r 12 000 and p I 6.0. In the third type of 2‐DE, employing urea and Nonidet P‐40 in the first and SDS in the second dimension, the plasma polypeptide composition was studied. The presence of an unidentified polypeptide could be confirmed on day 5, tending to disappear there‐after. This M r 12 000 component consists of two major spots at p I 5.7 and 6.0 and four minor ones between p I 6.0 and 8.0. These properties suggest that this protein corresponds to serum amyloid A apolipoprotein.