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Journal of Lipid Research, Vol 36, 890-900, Copyright © 1995 by Lipid Research, Inc.
L Kotite, N Bergeron and RJ Havel
We have developed a procedure to quantify apolipoprotein (apo) B-100,
apoB-48, and apoE in human triglyceride-rich lipoproteins. This procedure
permits delipidation of small amounts of triglyceride-rich lipoproteins
without appreciable losses, and quantification of these apolipoproteins in
samples containing as little as 10 micrograms of protein. Delipidated
triglyceride-rich lipoproteins are subjected to sodium dodecyl sulfate
polyacrylamide slab gel electrophoresis, and the mass of apolipoproteins is
estimated after densitometric scanning and volume integration of Coomassie
blue-stained bands. The chromogenicities of apoB-100 and apoB-48 are
virtually identical, and twofold lower than that of apoE. The standard
curve for each apolipoprotein follows a power function over a wide protein
range, permitting quantification of as little as 0.2 microgram of apoB-48
and as much as 30 micrograms of apoB-100 from a single application of
triglyceride-rich lipoproteins to the gels. This method is suitable for
routine use in studies of the intestinal and hepatic contributions to
triglyceride-rich lipoproteins and their responses to postprandial lipemia.
ARTICLES
Quantification of apolipoproteins B-100, B-48, and E in human triglyceride-rich lipoproteins
Cardiovascular Research Institute, University of California, San Francisco 94143-0130, USA.
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