Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Biochim Biophys Acta. 1983 Feb 7;750(2):317-21. doi: 10.1016/0005-2760(83)90034-6.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Apolipoproteins / blood*
  • Apolipoproteins / isolation & purification
  • Cholesterol / blood
  • Chromatography, Gel / methods
  • Humans
  • Immunodiffusion
  • Lipoproteins / blood*
  • Molecular Weight
  • Phospholipids / blood
  • Triglycerides / blood


  • Apolipoproteins
  • Lipoproteins
  • Phospholipids
  • Triglycerides
  • Cholesterol