Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Steven D. Carson

doi:10.1016/0005-2760(83)90034-6

Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Steven D. Carson

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

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 language	English (US)
Pages (from-to)	317-321
Number of pages	5
Journal	Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume	750
Issue number	2
DOIs	https://doi.org/10.1016/0005-2760(83)90034-6
State	Published - Feb 7 1983
Externally published	Yes

Keywords

Affinity chromatography: (Human plasma)
Apolipoprotein
Lipoprotein

ASJC Scopus subject areas

Biophysics
Biochemistry
Endocrinology

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10.1016/0005-2760(83)90034-6

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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.}",

note = "Funding Information: I thank Dr. Richard Have1 for the immunoassays of apolipoproteins A-II and E, and Larry Macala and Dr. R.K. Yu for the lipid analyses. I also thank Sharon Carson for excellent technical assistance and Liz Salvati for typing this manuscript. This research was supported in part by grant HL 22957 and S.D.C. was supported by Individual National Research Service Award 1 F32 HL 06034 from the National Heart, Lung and Blood Institute of NIH.",

year = "1983",

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doi = "10.1016/0005-2760(83)90034-6",

language = "English (US)",

volume = "750",

pages = "317--321",

journal = "Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism",

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TY - JOUR

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

AU - Carson, Steven D.

N1 - Funding Information: I thank Dr. Richard Have1 for the immunoassays of apolipoproteins A-II and E, and Larry Macala and Dr. R.K. Yu for the lipid analyses. I also thank Sharon Carson for excellent technical assistance and Liz Salvati for typing this manuscript. This research was supported in part by grant HL 22957 and S.D.C. was supported by Individual National Research Service Award 1 F32 HL 06034 from the National Heart, Lung and Blood Institute of NIH.

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

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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

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AN - SCOPUS:0020657747

SN - 0005-2760

VL - 750

SP - 317

EP - 321

JO - Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism

JF - Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism

IS - 2

ER -

Chromatographic depletion of lipoproteins from plasma and recovery of apolipoproteins

Abstract

Keywords

ASJC Scopus subject areas

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