Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 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
Volume750
Issue number2
DOIs
StatePublished - Feb 7 1983

Fingerprint

Apolipoproteins
Lipoproteins
Plasmas
Recovery
Apolipoprotein A-I
Adsorption
Propylene Glycol
Sphingomyelins
HDL Lipoproteins
Chromatography
Complex Mixtures
Phosphatidylcholines
LDL Lipoproteins
Purification
Triglycerides
Proteins
Cholesterol
phenyl-sepharose

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Endocrinology
  • Medicine(all)

Cite this

@article{ef761d0dc13d490da7976fb67840fd63,
title = "Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins",
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 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.",
keywords = "Affinity chromatography: (Human plasma), Apolipoprotein, Lipoprotein",
author = "Carson, {Steven D.}",
year = "1983",
month = "2",
day = "7",
doi = "10.1016/0005-2760(83)90034-6",
language = "English (US)",
volume = "750",
pages = "317--321",
journal = "Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids",
issn = "1388-1981",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

AU - Carson, Steven D.

PY - 1983/2/7

Y1 - 1983/2/7

N2 - 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.

AB - 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.

KW - Affinity chromatography: (Human plasma)

KW - Apolipoprotein

KW - Lipoprotein

UR - http://www.scopus.com/inward/record.url?scp=0020657747&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020657747&partnerID=8YFLogxK

U2 - 10.1016/0005-2760(83)90034-6

DO - 10.1016/0005-2760(83)90034-6

M3 - Article

C2 - 6407529

AN - SCOPUS:0020657747

VL - 750

SP - 317

EP - 321

JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

SN - 1388-1981

IS - 2

ER -