Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Steven D. Carson

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


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 β-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.

Original languageEnglish (US)
Pages (from-to)317-321
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Issue number2
StatePublished - Feb 7 1983
Externally publishedYes


  • Affinity chromatography: (Human plasma)
  • Apolipoprotein
  • Lipoprotein

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Endocrinology


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