Solubilization and partial purification of aromatase from chicken ovary
Aromatase, the cytochrome P-450 that converts androgen to estrogen, has been solubilized from chicken ovarian microsomes with the nonionic detergent Emuigen 913. Following chromatography on gel filtration, anion exchange, dye affinity, and hydrophobic media, ovarian aromatase is purified up to 27-fo...
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| Veröffentlicht in: | Journal of steroid biochemistry 1986-07, Vol.25 (1), p.91-97 |
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| container_end_page | 97 |
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| container_start_page | 91 |
| container_title | Journal of steroid biochemistry |
| container_volume | 25 |
| creator | Leshin, Mark Noble, Janet F. |
| description | Aromatase, the cytochrome P-450 that converts androgen to estrogen, has been solubilized from chicken ovarian microsomes with the nonionic detergent Emuigen 913. Following chromatography on gel filtration, anion exchange, dye affinity, and hydrophobic media, ovarian aromatase is purified up to 27-fold with 10–15% recovery. Separation of the cytochrome P-450 aromatase from NADPH cytochrome P-450 reductase is achieved during the purification. The partially purified enzyme is stable for as long as 6 months when frozen in liquid nitrogen in buffer containing dithiothreitol, glycerol, Emuigen and 150mM KCl. |
| doi_str_mv | 10.1016/0022-4731(86)90285-2 |
| format | Article |
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Following chromatography on gel filtration, anion exchange, dye affinity, and hydrophobic media, ovarian aromatase is purified up to 27-fold with 10–15% recovery. Separation of the cytochrome P-450 aromatase from NADPH cytochrome P-450 reductase is achieved during the purification. The partially purified enzyme is stable for as long as 6 months when frozen in liquid nitrogen in buffer containing dithiothreitol, glycerol, Emuigen and 150mM KCl.</description><identifier>ISSN: 0022-4731</identifier><identifier>DOI: 10.1016/0022-4731(86)90285-2</identifier><identifier>PMID: 3091941</identifier><identifier>CODEN: JSTBBK</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>Animals ; aromatase ; Aromatase - analysis ; Aromatase - isolation & purification ; Biological and medical sciences ; Chickens ; Chromatography, Affinity ; Chromatography, Gel ; Female ; Fundamental and applied biological sciences. Psychology ; Hormone metabolism and regulation ; Mammalian female genital system ; microsomes ; NADPH-Ferrihemoprotein Reductase - analysis ; ovary ; Ovary - enzymology ; Solubility ; Vertebrates: reproduction</subject><ispartof>Journal of steroid biochemistry, 1986-07, Vol.25 (1), p.91-97</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-a252cb1b9ad666a777e17ecd353846a0e2f147725ae680c60d94144862f726f83</citedby><cites>FETCH-LOGICAL-c417t-a252cb1b9ad666a777e17ecd353846a0e2f147725ae680c60d94144862f726f83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8071414$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3091941$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leshin, Mark</creatorcontrib><creatorcontrib>Noble, Janet F.</creatorcontrib><title>Solubilization and partial purification of aromatase from chicken ovary</title><title>Journal of steroid biochemistry</title><addtitle>J Steroid Biochem</addtitle><description>Aromatase, the cytochrome P-450 that converts androgen to estrogen, has been solubilized from chicken ovarian microsomes with the nonionic detergent Emuigen 913. Following chromatography on gel filtration, anion exchange, dye affinity, and hydrophobic media, ovarian aromatase is purified up to 27-fold with 10–15% recovery. Separation of the cytochrome P-450 aromatase from NADPH cytochrome P-450 reductase is achieved during the purification. The partially purified enzyme is stable for as long as 6 months when frozen in liquid nitrogen in buffer containing dithiothreitol, glycerol, Emuigen and 150mM KCl.</description><subject>Animals</subject><subject>aromatase</subject><subject>Aromatase - analysis</subject><subject>Aromatase - isolation & purification</subject><subject>Biological and medical sciences</subject><subject>Chickens</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone metabolism and regulation</subject><subject>Mammalian female genital system</subject><subject>microsomes</subject><subject>NADPH-Ferrihemoprotein Reductase - analysis</subject><subject>ovary</subject><subject>Ovary - enzymology</subject><subject>Solubility</subject><subject>Vertebrates: reproduction</subject><issn>0022-4731</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhnNQ_P4HCj2I6KGapGmSXgRZdBUED-o5TNMJRrvtmrQL-uvNusse9ZQh7zPDzEPIMaOXjDJ5RSnnuVAFO9fyoqJclznfInub712yH-M7pazSgu-QnYJWrBJsj0yf-3asfeu_YfB9l0HXZHMIg4c2m4_BO29XQe8yCP0MBoiYuVRl9s3bD0zJAsLXIdl20EY8Wr8H5PXu9mVynz8-TR8mN4-5FUwNOfCS25rVFTRSSlBKIVNom6IstJBAkTsmlOIloNTUStqkLYXQkjvFpdPFATlbzZ2H_nPEOJiZjxbbFjrsx2iUoqwUvPgXZKKUQrIygWIF2tDHGNCZefCzdJJh1CzlmqVFs7RotDS_cg1PbSfr-WM9w2bTtDab8tN1DtFC6wJ01scNpqli6bKEXa8wTNIWHoOJ1mNnsfEB7WCa3v-9xw-e15Z6</recordid><startdate>19860701</startdate><enddate>19860701</enddate><creator>Leshin, Mark</creator><creator>Noble, Janet F.</creator><general>Elsevier B.V</general><general>Pergamon</general><scope>IQODW</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19860701</creationdate><title>Solubilization and partial purification of aromatase from chicken ovary</title><author>Leshin, Mark ; Noble, Janet F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-a252cb1b9ad666a777e17ecd353846a0e2f147725ae680c60d94144862f726f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Animals</topic><topic>aromatase</topic><topic>Aromatase - analysis</topic><topic>Aromatase - isolation & purification</topic><topic>Biological and medical sciences</topic><topic>Chickens</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone metabolism and regulation</topic><topic>Mammalian female genital system</topic><topic>microsomes</topic><topic>NADPH-Ferrihemoprotein Reductase - analysis</topic><topic>ovary</topic><topic>Ovary - enzymology</topic><topic>Solubility</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leshin, Mark</creatorcontrib><creatorcontrib>Noble, Janet F.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of steroid biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leshin, Mark</au><au>Noble, Janet F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solubilization and partial purification of aromatase from chicken ovary</atitle><jtitle>Journal of steroid biochemistry</jtitle><addtitle>J Steroid Biochem</addtitle><date>1986-07-01</date><risdate>1986</risdate><volume>25</volume><issue>1</issue><spage>91</spage><epage>97</epage><pages>91-97</pages><issn>0022-4731</issn><coden>JSTBBK</coden><abstract>Aromatase, the cytochrome P-450 that converts androgen to estrogen, has been solubilized from chicken ovarian microsomes with the nonionic detergent Emuigen 913. Following chromatography on gel filtration, anion exchange, dye affinity, and hydrophobic media, ovarian aromatase is purified up to 27-fold with 10–15% recovery. Separation of the cytochrome P-450 aromatase from NADPH cytochrome P-450 reductase is achieved during the purification. The partially purified enzyme is stable for as long as 6 months when frozen in liquid nitrogen in buffer containing dithiothreitol, glycerol, Emuigen and 150mM KCl.</abstract><cop>Oxford</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>3091941</pmid><doi>10.1016/0022-4731(86)90285-2</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-4731 |
| ispartof | Journal of steroid biochemistry, 1986-07, Vol.25 (1), p.91-97 |
| issn | 0022-4731 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals aromatase Aromatase - analysis Aromatase - isolation & purification Biological and medical sciences Chickens Chromatography, Affinity Chromatography, Gel Female Fundamental and applied biological sciences. Psychology Hormone metabolism and regulation Mammalian female genital system microsomes NADPH-Ferrihemoprotein Reductase - analysis ovary Ovary - enzymology Solubility Vertebrates: reproduction |
| title | Solubilization and partial purification of aromatase from chicken ovary |
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