Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins.
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.
D001053:Apolipoproteins / Q000097:blood* / Q000302:isolation & purification; D002784:Cholesterol / Q000097:blood; D002850:Chromatography, Gel / Q000379:methods; D006801:Humans; D005779:Immunodiffusion; D008074:Lipoproteins / Q000097:blood*; D008970:Molecular Weight; D010743:Phospholipids / Q000097:blood; D014280:Triglycerides / Q000097:blood
D001053:Apolipoproteins; D008074:Lipoproteins; D010743:Phospholipids; D014280:Triglycerides; D002784:Cholesterol