Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties
Arachidonic acid 15-lipoxygenase was purified from rabbit peritoneal polymorphonuclear leukocytes. The enzyme was recovered in the cytosol fraction after sonication and purified about 250-fold by acetone precipitation, column chromatography on CM52, Sephadex G-150, and hydroxyapatite. The enzyme cat...
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| Veröffentlicht in: | The Journal of biological chemistry 1981-09, Vol.256 (18), p.9583-9592 |
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| creator | Narumiya, S Salmon, J A Cottee, F H Weatherley, B C Flower, R J |
| description | Arachidonic acid 15-lipoxygenase was purified from rabbit peritoneal polymorphonuclear leukocytes. The enzyme was recovered
in the cytosol fraction after sonication and purified about 250-fold by acetone precipitation, column chromatography on CM52,
Sephadex G-150, and hydroxyapatite. The enzyme catalyzed the conversion of arachidonic acid to 15-hydroperoxy-5,8,11,13-eicosatetraenoic
acid (15-HPETE), which then decomposed to a mixture of 15-hydroxy-5,8,11,13-eicosatetraenoic acid (15-HETE), 15-keto-5,8,11,13-eicosatetraenoic
acid, 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid, and 11,14,15-trihydroxy-5,8,12-eicosatrienoic acid. The enzyme was
specific for oxygenation at carbon 15 of arachidonic acid. The apparent molecular weight of the enzyme was about 61,000 as
measured by Sephadex G-150 gel filtration chromatography. The enzyme was sensitive to sulfhydryl-blocking reagents such as
p-chloromercuribenzoic acid. The enzyme activity was inhibited by eicosatetraynoic acid (ETYA) or 3-amino-1-(m-(trifluoromethyl)-phenyl)2-pyrazoline
(BW755C), but not by indomethacin up to 200 micrograms/ml. |
| doi_str_mv | 10.1016/s0021-9258(19)68802-2 |
| format | Article |
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in the cytosol fraction after sonication and purified about 250-fold by acetone precipitation, column chromatography on CM52,
Sephadex G-150, and hydroxyapatite. The enzyme catalyzed the conversion of arachidonic acid to 15-hydroperoxy-5,8,11,13-eicosatetraenoic
acid (15-HPETE), which then decomposed to a mixture of 15-hydroxy-5,8,11,13-eicosatetraenoic acid (15-HETE), 15-keto-5,8,11,13-eicosatetraenoic
acid, 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid, and 11,14,15-trihydroxy-5,8,12-eicosatrienoic acid. The enzyme was
specific for oxygenation at carbon 15 of arachidonic acid. The apparent molecular weight of the enzyme was about 61,000 as
measured by Sephadex G-150 gel filtration chromatography. The enzyme was sensitive to sulfhydryl-blocking reagents such as
p-chloromercuribenzoic acid. The enzyme activity was inhibited by eicosatetraynoic acid (ETYA) or 3-amino-1-(m-(trifluoromethyl)-phenyl)2-pyrazoline
(BW755C), but not by indomethacin up to 200 micrograms/ml.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)68802-2</identifier><identifier>PMID: 6793572</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Arachidonate Lipoxygenases ; Arachidonic Acid ; Arachidonic Acids - blood ; Cations, Divalent ; Chromatography, High Pressure Liquid ; Kinetics ; leukocytes ; lipoxygenase ; Lipoxygenase - blood ; Lipoxygenase - isolation & purification ; Mass Spectrometry ; Molecular Weight ; Neutrophils - enzymology ; purification ; Rabbits</subject><ispartof>The Journal of biological chemistry, 1981-09, Vol.256 (18), p.9583-9592</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-c88246ccee4519e727e1d7337698b900338daed3a9a0564711254d8a5aecec3f3</citedby><cites>FETCH-LOGICAL-c476t-c88246ccee4519e727e1d7337698b900338daed3a9a0564711254d8a5aecec3f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6793572$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Narumiya, S</creatorcontrib><creatorcontrib>Salmon, J A</creatorcontrib><creatorcontrib>Cottee, F H</creatorcontrib><creatorcontrib>Weatherley, B C</creatorcontrib><creatorcontrib>Flower, R J</creatorcontrib><title>Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Arachidonic acid 15-lipoxygenase was purified from rabbit peritoneal polymorphonuclear leukocytes. The enzyme was recovered
in the cytosol fraction after sonication and purified about 250-fold by acetone precipitation, column chromatography on CM52,
Sephadex G-150, and hydroxyapatite. The enzyme catalyzed the conversion of arachidonic acid to 15-hydroperoxy-5,8,11,13-eicosatetraenoic
acid (15-HPETE), which then decomposed to a mixture of 15-hydroxy-5,8,11,13-eicosatetraenoic acid (15-HETE), 15-keto-5,8,11,13-eicosatetraenoic
acid, 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid, and 11,14,15-trihydroxy-5,8,12-eicosatrienoic acid. The enzyme was
specific for oxygenation at carbon 15 of arachidonic acid. The apparent molecular weight of the enzyme was about 61,000 as
measured by Sephadex G-150 gel filtration chromatography. The enzyme was sensitive to sulfhydryl-blocking reagents such as
p-chloromercuribenzoic acid. The enzyme activity was inhibited by eicosatetraynoic acid (ETYA) or 3-amino-1-(m-(trifluoromethyl)-phenyl)2-pyrazoline
(BW755C), but not by indomethacin up to 200 micrograms/ml.</description><subject>Animals</subject><subject>Arachidonate Lipoxygenases</subject><subject>Arachidonic Acid</subject><subject>Arachidonic Acids - blood</subject><subject>Cations, Divalent</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Kinetics</subject><subject>leukocytes</subject><subject>lipoxygenase</subject><subject>Lipoxygenase - blood</subject><subject>Lipoxygenase - isolation & purification</subject><subject>Mass Spectrometry</subject><subject>Molecular Weight</subject><subject>Neutrophils - enzymology</subject><subject>purification</subject><subject>Rabbits</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1L3UAUxYfSYp_aP0EYEIpdROcj87UU0VoQLFTB3TCZ3Jhpk0ycSbD5783re7jt3dzF-d174ByETig5p4TKi0wIo4VhQp9R801qTVjBPqANJZoXXNCnj2jzjnxGhzn_JuuUhh6gA6kMF4pt0HKZnG9DHYfgsfOhxlQUXRjj3-UZBpcBNyn2OLmqChMeIYUpDuA6PMZu6WMa2zjMvgOXcAfzn-iXCfI5_unSFLbUnEITvJtCHLAbajymuD6ZAuRj9KlxXYYv-32EHm-uH65ui7v77z-uLu8KXyo5FV5rVkrvAUpBDSimgNaKcyWNrgwhnOvaQc2dcUTIUlHKRFlrJxx48LzhR-jr7u9q_TJDnmwfsoeucwPEOVvFpS6VUv8FqeDSCFGuoNiBPsWcEzR2TKF3abGU2G039tc2eLsN3lJj_3Vj2Xp3sjeYqx7q96t9Gat-utPb8Ny-hgS2CtG30FsmpKXaGqE5fwMBXZiJ</recordid><startdate>19810925</startdate><enddate>19810925</enddate><creator>Narumiya, S</creator><creator>Salmon, J A</creator><creator>Cottee, F H</creator><creator>Weatherley, B C</creator><creator>Flower, R J</creator><general>American Society for Biochemistry and Molecular Biology</general><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>19810925</creationdate><title>Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties</title><author>Narumiya, S ; Salmon, J A ; Cottee, F H ; Weatherley, B C ; Flower, R J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-c88246ccee4519e727e1d7337698b900338daed3a9a0564711254d8a5aecec3f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Animals</topic><topic>Arachidonate Lipoxygenases</topic><topic>Arachidonic Acid</topic><topic>Arachidonic Acids - blood</topic><topic>Cations, Divalent</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Kinetics</topic><topic>leukocytes</topic><topic>lipoxygenase</topic><topic>Lipoxygenase - blood</topic><topic>Lipoxygenase - isolation & purification</topic><topic>Mass Spectrometry</topic><topic>Molecular Weight</topic><topic>Neutrophils - enzymology</topic><topic>purification</topic><topic>Rabbits</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Narumiya, S</creatorcontrib><creatorcontrib>Salmon, J A</creatorcontrib><creatorcontrib>Cottee, F H</creatorcontrib><creatorcontrib>Weatherley, B C</creatorcontrib><creatorcontrib>Flower, R J</creatorcontrib><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Narumiya, S</au><au>Salmon, J A</au><au>Cottee, F H</au><au>Weatherley, B C</au><au>Flower, R J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1981-09-25</date><risdate>1981</risdate><volume>256</volume><issue>18</issue><spage>9583</spage><epage>9592</epage><pages>9583-9592</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Arachidonic acid 15-lipoxygenase was purified from rabbit peritoneal polymorphonuclear leukocytes. The enzyme was recovered
in the cytosol fraction after sonication and purified about 250-fold by acetone precipitation, column chromatography on CM52,
Sephadex G-150, and hydroxyapatite. The enzyme catalyzed the conversion of arachidonic acid to 15-hydroperoxy-5,8,11,13-eicosatetraenoic
acid (15-HPETE), which then decomposed to a mixture of 15-hydroxy-5,8,11,13-eicosatetraenoic acid (15-HETE), 15-keto-5,8,11,13-eicosatetraenoic
acid, 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid, and 11,14,15-trihydroxy-5,8,12-eicosatrienoic acid. The enzyme was
specific for oxygenation at carbon 15 of arachidonic acid. The apparent molecular weight of the enzyme was about 61,000 as
measured by Sephadex G-150 gel filtration chromatography. The enzyme was sensitive to sulfhydryl-blocking reagents such as
p-chloromercuribenzoic acid. The enzyme activity was inhibited by eicosatetraynoic acid (ETYA) or 3-amino-1-(m-(trifluoromethyl)-phenyl)2-pyrazoline
(BW755C), but not by indomethacin up to 200 micrograms/ml.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6793572</pmid><doi>10.1016/s0021-9258(19)68802-2</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Arachidonate Lipoxygenases Arachidonic Acid Arachidonic Acids - blood Cations, Divalent Chromatography, High Pressure Liquid Kinetics leukocytes lipoxygenase Lipoxygenase - blood Lipoxygenase - isolation & purification Mass Spectrometry Molecular Weight Neutrophils - enzymology purification Rabbits |
| title | Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties |
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