Isolation of pure LpB from human serum.
Low density lipoproteins (LDL), even after isolation from a narrow density cut and after several washes by preparative ultracentrifugation, are contaminated by 3-5% non-apoB proteins. Incubation of these LDL with artificial triglyceride-rich lipid emulsions (TGRP) removed all contaminating apoC and...
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1988-08-01
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doaj-05cf2e7530464353aeb5725587c538f32021-04-25T04:21:10ZengElsevierJournal of Lipid Research0022-22751988-08-01276681686Isolation of pure LpB from human serum.R ZechnerR MoserG M KostnerLow density lipoproteins (LDL), even after isolation from a narrow density cut and after several washes by preparative ultracentrifugation, are contaminated by 3-5% non-apoB proteins. Incubation of these LDL with artificial triglyceride-rich lipid emulsions (TGRP) removed all contaminating apoC and also, under certain conditions, apoA proteins. TGRP treatment did not, however, change the lipid composition and the flotation behavior of LDL. Residual apoE and albumin, amounting up to 0.5% of the apoB mass, were resistant to removal by TGRP treatment as well as by heparin-Sepharose column chromatography. ApoE and albumin could only be removed by immunoabsorption.http://www.sciencedirect.com/science/article/pii/S0022227520388076 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
R Zechner R Moser G M Kostner |
spellingShingle |
R Zechner R Moser G M Kostner Isolation of pure LpB from human serum. Journal of Lipid Research |
author_facet |
R Zechner R Moser G M Kostner |
author_sort |
R Zechner |
title |
Isolation of pure LpB from human serum. |
title_short |
Isolation of pure LpB from human serum. |
title_full |
Isolation of pure LpB from human serum. |
title_fullStr |
Isolation of pure LpB from human serum. |
title_full_unstemmed |
Isolation of pure LpB from human serum. |
title_sort |
isolation of pure lpb from human serum. |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
1988-08-01 |
description |
Low density lipoproteins (LDL), even after isolation from a narrow density cut and after several washes by preparative ultracentrifugation, are contaminated by 3-5% non-apoB proteins. Incubation of these LDL with artificial triglyceride-rich lipid emulsions (TGRP) removed all contaminating apoC and also, under certain conditions, apoA proteins. TGRP treatment did not, however, change the lipid composition and the flotation behavior of LDL. Residual apoE and albumin, amounting up to 0.5% of the apoB mass, were resistant to removal by TGRP treatment as well as by heparin-Sepharose column chromatography. ApoE and albumin could only be removed by immunoabsorption. |
url |
http://www.sciencedirect.com/science/article/pii/S0022227520388076 |
work_keys_str_mv |
AT rzechner isolationofpurelpbfromhumanserum AT rmoser isolationofpurelpbfromhumanserum AT gmkostner isolationofpurelpbfromhumanserum |
_version_ |
1721510291641991168 |