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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Main Authors: S K Erickson, B Bösterling
Format: Article
Language:English
Published: Elsevier 1981-07-01
Series:Journal of Lipid Research
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520373600
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spelling 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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