Labeling of high density lipoproteins with [3H] acetic anhydride
Rat serum HDL was labeled by reaction with [3H] acetic anhydride at pH 7.2 for 30 min at room temperature by a modification of the method of Montelaro and Rueckert (1975. J. Biol. Chem. 250: 1413). Protein specific activities of 60 dpm/ng were achieved. Seven percent of the label was in lipid, of wh...
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Format: | Article |
Language: | English |
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Elsevier
1978-01-01
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Series: | Journal of Lipid Research |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520415822 |
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author | J B Marsh |
author_facet | J B Marsh |
author_sort | J B Marsh |
collection | DOAJ |
description | Rat serum HDL was labeled by reaction with [3H] acetic anhydride at pH 7.2 for 30 min at room temperature by a modification of the method of Montelaro and Rueckert (1975. J. Biol. Chem. 250: 1413). Protein specific activities of 60 dpm/ng were achieved. Seven percent of the label was in lipid, of which 92% was recovered in phospholipid. The labeled HDL migrated as a single band as seen by electrophoretic or column chromatographic analysis. When the labeled HDL was injected into rats without re-isolation, the biological half-life was not significantly different from HDL labeled in vitro with 125I or in vivo with amino acids. All of the apoproteins were labeled; their specific activities were closer to one another than those obtained with 125I. For some applications, acetylation may provide a useful alternative to the 125I labeling procedure. |
first_indexed | 2024-12-17T07:31:52Z |
format | Article |
id | doaj.art-844072f7c6954ca1969382f070d83dfb |
institution | Directory Open Access Journal |
issn | 0022-2275 |
language | English |
last_indexed | 2024-12-17T07:31:52Z |
publishDate | 1978-01-01 |
publisher | Elsevier |
record_format | Article |
series | Journal of Lipid Research |
spelling | doaj.art-844072f7c6954ca1969382f070d83dfb2022-12-21T21:58:28ZengElsevierJournal of Lipid Research0022-22751978-01-01191107110Labeling of high density lipoproteins with [3H] acetic anhydrideJ B Marsh0Department of Physiology and Biochemistry, The Medical College of Pennsylvania, Philadelphia, PA 19129Rat serum HDL was labeled by reaction with [3H] acetic anhydride at pH 7.2 for 30 min at room temperature by a modification of the method of Montelaro and Rueckert (1975. J. Biol. Chem. 250: 1413). Protein specific activities of 60 dpm/ng were achieved. Seven percent of the label was in lipid, of which 92% was recovered in phospholipid. The labeled HDL migrated as a single band as seen by electrophoretic or column chromatographic analysis. When the labeled HDL was injected into rats without re-isolation, the biological half-life was not significantly different from HDL labeled in vitro with 125I or in vivo with amino acids. All of the apoproteins were labeled; their specific activities were closer to one another than those obtained with 125I. For some applications, acetylation may provide a useful alternative to the 125I labeling procedure.http://www.sciencedirect.com/science/article/pii/S0022227520415822In vitro labelinglipoprotein turnoverphospholipid labeling |
spellingShingle | J B Marsh Labeling of high density lipoproteins with [3H] acetic anhydride Journal of Lipid Research In vitro labeling lipoprotein turnover phospholipid labeling |
title | Labeling of high density lipoproteins with [3H] acetic anhydride |
title_full | Labeling of high density lipoproteins with [3H] acetic anhydride |
title_fullStr | Labeling of high density lipoproteins with [3H] acetic anhydride |
title_full_unstemmed | Labeling of high density lipoproteins with [3H] acetic anhydride |
title_short | Labeling of high density lipoproteins with [3H] acetic anhydride |
title_sort | labeling of high density lipoproteins with 3h acetic anhydride |
topic | In vitro labeling lipoprotein turnover phospholipid labeling |
url | http://www.sciencedirect.com/science/article/pii/S0022227520415822 |
work_keys_str_mv | AT jbmarsh labelingofhighdensitylipoproteinswith3haceticanhydride |