PMID: 6407529Feb 7, 1983Paper

Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Biochimica Et Biophysica Acta
S D Carson

Abstract

Selective adsorption of proteins from a complex mixture onto an affinity support presents a very powerful approach to protein purification. High density lipoprotein (HDL) and low density lipoprotein (LDL) have been removed from plasma by hydrophobic adsorption chromatography using phenyl-Sepharose. Plasma chromatographed on phenyl-Sepharose is depleted of beta-lipoprotein and apolipoproteins A-I, A-II and E. Less than 5% of the initial amounts of cholesterol, triacylglycerol, sphingomyelin, and phosphatidylcholine remain in the plasma. Column elution with propylene glycol permits recovery of apolipoproteins A-I, A-II and E. This procedure should provide a convenient alternative to ultracentrifugal removal of lipoproteins from plasma.

References

Jul 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·M R Rifkin
Jan 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·W Stoffel, T Demant

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