Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol
12alpha-Hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol was studied in reconstituted systems consisting of electrophoretically homogeneous cytochrome P-450 LM4 fractions and NADPH-cytochrome P-450 reductase from rabbit liver microsomes. Cytochrome P-450 LM4 fractions were prepared from untreat...
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| Veröffentlicht in: | European journal of biochemistry 1982-07, Vol.125 (2), p.423-429 |
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| creator | Hansson, R Wikvall, K |
| description | 12alpha-Hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol was studied in reconstituted systems consisting of electrophoretically homogeneous cytochrome P-450 LM4 fractions and NADPH-cytochrome P-450 reductase from rabbit liver microsomes. Cytochrome P-450 LM4 fractions were prepared from untreated, phenobarbital-treated, beta-naphthoflavone-treated and starved rabbits. The purified cytochromes catalyzed 12alpha-hydroxylation more efficiently than the corresponding microsomes. In the reconstituted systems, carbon monoxide inhibited 12alpha-hydroxylation by 50-80%. The rate of 12alpha-hydroxylation was three to four times higher with cytochrome P-450 LM4 fractions from starved rabbits than with cytochrome P-450 LM4 fractions from untreated, phenobarbital-treated and beta-naphthoflavone-treated animals. Amino acid analyses, peptide mapping experiments as well as absorption spectral and circular dichroism spectral analyses revealed physical differences between cytochrome P-450 LM4 fractions from starved animals and preparations from phenobarbital-treated animals. The results indicate the presence of a cytochrome P-450 species in the cytochrome P-450 LM4 fraction specific for 12alpha-hydroxylation. |
| doi_str_mv | 10.1111/j.1432-1033.1982.tb06700.x |
| format | Article |
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Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Hansson, R ; Wikvall, K</creator><creatorcontrib>Hansson, R ; Wikvall, K</creatorcontrib><description>12alpha-Hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol was studied in reconstituted systems consisting of electrophoretically homogeneous cytochrome P-450 LM4 fractions and NADPH-cytochrome P-450 reductase from rabbit liver microsomes. Cytochrome P-450 LM4 fractions were prepared from untreated, phenobarbital-treated, beta-naphthoflavone-treated and starved rabbits. The purified cytochromes catalyzed 12alpha-hydroxylation more efficiently than the corresponding microsomes. In the reconstituted systems, carbon monoxide inhibited 12alpha-hydroxylation by 50-80%. The rate of 12alpha-hydroxylation was three to four times higher with cytochrome P-450 LM4 fractions from starved rabbits than with cytochrome P-450 LM4 fractions from untreated, phenobarbital-treated and beta-naphthoflavone-treated animals. Amino acid analyses, peptide mapping experiments as well as absorption spectral and circular dichroism spectral analyses revealed physical differences between cytochrome P-450 LM4 fractions from starved animals and preparations from phenobarbital-treated animals. The results indicate the presence of a cytochrome P-450 species in the cytochrome P-450 LM4 fraction specific for 12alpha-hydroxylation.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1982.tb06700.x</identifier><identifier>PMID: 6811268</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Benzoflavones - metabolism ; Benzoflavones - pharmacology ; beta-Naphthoflavone ; Bile Acids and Salts - biosynthesis ; Catalysis ; Cytochrome P-450 Enzyme System - metabolism ; Flavonoids - metabolism ; Hydroxylation ; Microsomes, Liver - enzymology ; NADPH-Ferrihemoprotein Reductase - metabolism ; Phenobarbital - pharmacology ; Rabbits ; Starvation - metabolism</subject><ispartof>European journal of biochemistry, 1982-07, Vol.125 (2), p.423-429</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1618-40117b1d40fc8b58b36c510c609432be3e837336abf5a001370b119f200d887d3</citedby><cites>FETCH-LOGICAL-c1618-40117b1d40fc8b58b36c510c609432be3e837336abf5a001370b119f200d887d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6811268$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hansson, R</creatorcontrib><creatorcontrib>Wikvall, K</creatorcontrib><title>Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>12alpha-Hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol was studied in reconstituted systems consisting of electrophoretically homogeneous cytochrome P-450 LM4 fractions and NADPH-cytochrome P-450 reductase from rabbit liver microsomes. Cytochrome P-450 LM4 fractions were prepared from untreated, phenobarbital-treated, beta-naphthoflavone-treated and starved rabbits. The purified cytochromes catalyzed 12alpha-hydroxylation more efficiently than the corresponding microsomes. In the reconstituted systems, carbon monoxide inhibited 12alpha-hydroxylation by 50-80%. The rate of 12alpha-hydroxylation was three to four times higher with cytochrome P-450 LM4 fractions from starved rabbits than with cytochrome P-450 LM4 fractions from untreated, phenobarbital-treated and beta-naphthoflavone-treated animals. Amino acid analyses, peptide mapping experiments as well as absorption spectral and circular dichroism spectral analyses revealed physical differences between cytochrome P-450 LM4 fractions from starved animals and preparations from phenobarbital-treated animals. The results indicate the presence of a cytochrome P-450 species in the cytochrome P-450 LM4 fraction specific for 12alpha-hydroxylation.</description><subject>Animals</subject><subject>Benzoflavones - metabolism</subject><subject>Benzoflavones - pharmacology</subject><subject>beta-Naphthoflavone</subject><subject>Bile Acids and Salts - biosynthesis</subject><subject>Catalysis</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Flavonoids - metabolism</subject><subject>Hydroxylation</subject><subject>Microsomes, Liver - enzymology</subject><subject>NADPH-Ferrihemoprotein Reductase - metabolism</subject><subject>Phenobarbital - pharmacology</subject><subject>Rabbits</subject><subject>Starvation - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNUU2L2zAQFaVLNs32JyyIHnqq3BnLluTeSug2CynbQ_csJFnGDo6VWg7E9_3ha29C2LkMw7w3H-8R8gUhwSm-7xLMeMoQOE-wUGkyWBASIDl9IMtr6yNZAmDG0iIXt-RTjDsAEIWQC7IQCjEVakleNmPZh9PYmqEJXaRNR20T4tgNtY9NpKGa6tZT45oyJnQ9DsHVfdh7-pdlOdDtn4yarqSYmvZQG1a_Hzezc-sHw1wdWh8H03nG34DfqDwTyia0d-SmMm30ny95RZ4ffv1bb9j26ffj-ueWORSoWAaI0mKZQeWUzZXlwuUITkAx_Ww994pLzoWxVW6m17kEi1hUKUCplCz5inw9zz304f9xukfvm-h82053hWPUMktTDiAn4I8z0PUhxt5X-tA3e9OPGkHPFuidnnXWs856tkBfLNCniXx_2XK0e19eqRfN-SudeoKl</recordid><startdate>198207</startdate><enddate>198207</enddate><creator>Hansson, R</creator><creator>Wikvall, K</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>198207</creationdate><title>Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol</title><author>Hansson, R ; Wikvall, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1618-40117b1d40fc8b58b36c510c609432be3e837336abf5a001370b119f200d887d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Benzoflavones - metabolism</topic><topic>Benzoflavones - pharmacology</topic><topic>beta-Naphthoflavone</topic><topic>Bile Acids and Salts - biosynthesis</topic><topic>Catalysis</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>Flavonoids - metabolism</topic><topic>Hydroxylation</topic><topic>Microsomes, Liver - enzymology</topic><topic>NADPH-Ferrihemoprotein Reductase - metabolism</topic><topic>Phenobarbital - pharmacology</topic><topic>Rabbits</topic><topic>Starvation - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hansson, R</creatorcontrib><creatorcontrib>Wikvall, K</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hansson, R</au><au>Wikvall, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1982-07</date><risdate>1982</risdate><volume>125</volume><issue>2</issue><spage>423</spage><epage>429</epage><pages>423-429</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>12alpha-Hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol was studied in reconstituted systems consisting of electrophoretically homogeneous cytochrome P-450 LM4 fractions and NADPH-cytochrome P-450 reductase from rabbit liver microsomes. Cytochrome P-450 LM4 fractions were prepared from untreated, phenobarbital-treated, beta-naphthoflavone-treated and starved rabbits. The purified cytochromes catalyzed 12alpha-hydroxylation more efficiently than the corresponding microsomes. In the reconstituted systems, carbon monoxide inhibited 12alpha-hydroxylation by 50-80%. The rate of 12alpha-hydroxylation was three to four times higher with cytochrome P-450 LM4 fractions from starved rabbits than with cytochrome P-450 LM4 fractions from untreated, phenobarbital-treated and beta-naphthoflavone-treated animals. Amino acid analyses, peptide mapping experiments as well as absorption spectral and circular dichroism spectral analyses revealed physical differences between cytochrome P-450 LM4 fractions from starved animals and preparations from phenobarbital-treated animals. The results indicate the presence of a cytochrome P-450 species in the cytochrome P-450 LM4 fraction specific for 12alpha-hydroxylation.</abstract><cop>England</cop><pmid>6811268</pmid><doi>10.1111/j.1432-1033.1982.tb06700.x</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1982-07, Vol.125 (2), p.423-429 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74223007 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Benzoflavones - metabolism Benzoflavones - pharmacology beta-Naphthoflavone Bile Acids and Salts - biosynthesis Catalysis Cytochrome P-450 Enzyme System - metabolism Flavonoids - metabolism Hydroxylation Microsomes, Liver - enzymology NADPH-Ferrihemoprotein Reductase - metabolism Phenobarbital - pharmacology Rabbits Starvation - metabolism |
| title | Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol |
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