Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles.
Cholesterol 7 alpha-hydroxylase, the rate-limiting enzyme for bile acid synthesis, was shown to be copurified with human liver microsomal cytochrome P-450. When these cytochrome P-450 species were reconstituted in phospholipid-cholesterol vesicles together with NADPH-cytochrome P-450 reductase, high...
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Elsevier
1981-07-01
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Series: | Journal of Lipid Research |
Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520373600 |
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doaj-bdbcd61220b14d0ea2693b91d15a41a62021-04-24T05:50:11ZengElsevierJournal of Lipid Research0022-22751981-07-01225872876Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles.S K EricksonB BösterlingCholesterol 7 alpha-hydroxylase, the rate-limiting enzyme for bile acid synthesis, was shown to be copurified with human liver microsomal cytochrome P-450. When these cytochrome P-450 species were reconstituted in phospholipid-cholesterol vesicles together with NADPH-cytochrome P-450 reductase, high cholesterol 7 alpha-hydroxylase activity was obtained in the presence of NADPH. The activity represented a twofold enrichment relative to cytochrome P-450 and 43-fold enrichment relative to total microsomal protein. Availability of such a preparation will allow further characterization of the enzyme and will also allow studies of its mechanisms of regulation.http://www.sciencedirect.com/science/article/pii/S0022227520373600 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
S K Erickson B Bösterling |
spellingShingle |
S K Erickson B Bösterling Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. Journal of Lipid Research |
author_facet |
S K Erickson B Bösterling |
author_sort |
S K Erickson |
title |
Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |
title_short |
Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |
title_full |
Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |
title_fullStr |
Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |
title_full_unstemmed |
Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |
title_sort |
cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
1981-07-01 |
description |
Cholesterol 7 alpha-hydroxylase, the rate-limiting enzyme for bile acid synthesis, was shown to be copurified with human liver microsomal cytochrome P-450. When these cytochrome P-450 species were reconstituted in phospholipid-cholesterol vesicles together with NADPH-cytochrome P-450 reductase, high cholesterol 7 alpha-hydroxylase activity was obtained in the presence of NADPH. The activity represented a twofold enrichment relative to cytochrome P-450 and 43-fold enrichment relative to total microsomal protein. Availability of such a preparation will allow further characterization of the enzyme and will also allow studies of its mechanisms of regulation. |
url |
http://www.sciencedirect.com/science/article/pii/S0022227520373600 |
work_keys_str_mv |
AT skerickson cholesterol7alphahydroxylasefromhumanliverpartialpurificationandreconstructionintodefinedphospholipidcholesterolvesicles AT bbosterling cholesterol7alphahydroxylasefromhumanliverpartialpurificationandreconstructionintodefinedphospholipidcholesterolvesicles |
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1721511818711531520 |