Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria
l -Amino acid oxidase has been crystallized from extracts of rat kidney mitochondria. Purification involved sonic extraction, ammonium sulfate fractionation, chromatography on diethylaminoethyl cellulose, and gel filtration through Sephadex G-200. The enzyme revealed a single protein band on starch...
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| Veröffentlicht in: | The Journal of biological chemistry 1966-05, Vol.241 (9), p.2075-2083 |
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| container_title | The Journal of biological chemistry |
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| creator | Nakano, M Danowski, T S |
| description | l -Amino acid oxidase has been crystallized from extracts of rat kidney mitochondria. Purification involved sonic extraction,
ammonium sulfate fractionation, chromatography on diethylaminoethyl cellulose, and gel filtration through Sephadex G-200.
The enzyme revealed a single protein band on starch gel electrophoresis and exhibited a single homogeneous peak ( s 20, w 0 = 10.5 S) in an ultracentrifuge.
The enzyme is a flavoprotein in which the prosthetic group appears to be flavin mononucleotide. On the basis of the flavin
mononucleotide content of the enzyme (0.92%) and its molecular weight (88,900 ± 1,100), it has been concluded that the enzyme
contains 2 moles of flavin mononucleotide per mole.
The enzyme catalyzes the oxidation of many α-aminomonocarboxylic and α-hydroxy acids ( l configuration) but has no action on optically inactive acids such as glycine and α-hydroxyisobutyric acid. The turnover numbers
for the oxidation of l -leucine and of l -lactic acid were 6.3 and 26 moles per min per mole of flavin mononucleotide conjugated with enzyme, respectively. |
| doi_str_mv | 10.1016/S0021-9258(18)96668-8 |
| format | Article |
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ammonium sulfate fractionation, chromatography on diethylaminoethyl cellulose, and gel filtration through Sephadex G-200.
The enzyme revealed a single protein band on starch gel electrophoresis and exhibited a single homogeneous peak ( s 20, w 0 = 10.5 S) in an ultracentrifuge.
The enzyme is a flavoprotein in which the prosthetic group appears to be flavin mononucleotide. On the basis of the flavin
mononucleotide content of the enzyme (0.92%) and its molecular weight (88,900 ± 1,100), it has been concluded that the enzyme
contains 2 moles of flavin mononucleotide per mole.
The enzyme catalyzes the oxidation of many α-aminomonocarboxylic and α-hydroxy acids ( l configuration) but has no action on optically inactive acids such as glycine and α-hydroxyisobutyric acid. The turnover numbers
for the oxidation of l -leucine and of l -lactic acid were 6.3 and 26 moles per min per mole of flavin mononucleotide conjugated with enzyme, respectively.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)96668-8</identifier><identifier>PMID: 5946631</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Oxidoreductases - metabolism ; Animals ; Chemistry Techniques, Analytical ; Chromatography, Gel ; Crystallization ; Electrophoresis ; Flavin Mononucleotide ; Glycine - metabolism ; Hydroxybutyrates - metabolism ; In Vitro Techniques ; Kidney - cytology ; Kidney - enzymology ; Lactates - metabolism ; Leucine - metabolism ; Mitochondria - enzymology ; Rats</subject><ispartof>The Journal of biological chemistry, 1966-05, Vol.241 (9), p.2075-2083</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-cf8c56aa42d6ce0886e1b63726bd8a67ec656fb2a60eb79b51fc5970e8d456723</citedby><cites>FETCH-LOGICAL-c378t-cf8c56aa42d6ce0886e1b63726bd8a67ec656fb2a60eb79b51fc5970e8d456723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5946631$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakano, M</creatorcontrib><creatorcontrib>Danowski, T S</creatorcontrib><title>Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>l -Amino acid oxidase has been crystallized from extracts of rat kidney mitochondria. Purification involved sonic extraction,
ammonium sulfate fractionation, chromatography on diethylaminoethyl cellulose, and gel filtration through Sephadex G-200.
The enzyme revealed a single protein band on starch gel electrophoresis and exhibited a single homogeneous peak ( s 20, w 0 = 10.5 S) in an ultracentrifuge.
The enzyme is a flavoprotein in which the prosthetic group appears to be flavin mononucleotide. On the basis of the flavin
mononucleotide content of the enzyme (0.92%) and its molecular weight (88,900 ± 1,100), it has been concluded that the enzyme
contains 2 moles of flavin mononucleotide per mole.
The enzyme catalyzes the oxidation of many α-aminomonocarboxylic and α-hydroxy acids ( l configuration) but has no action on optically inactive acids such as glycine and α-hydroxyisobutyric acid. The turnover numbers
for the oxidation of l -leucine and of l -lactic acid were 6.3 and 26 moles per min per mole of flavin mononucleotide conjugated with enzyme, respectively.</description><subject>Amino Acid Oxidoreductases - metabolism</subject><subject>Animals</subject><subject>Chemistry Techniques, Analytical</subject><subject>Chromatography, Gel</subject><subject>Crystallization</subject><subject>Electrophoresis</subject><subject>Flavin Mononucleotide</subject><subject>Glycine - metabolism</subject><subject>Hydroxybutyrates - metabolism</subject><subject>In Vitro Techniques</subject><subject>Kidney - cytology</subject><subject>Kidney - enzymology</subject><subject>Lactates - metabolism</subject><subject>Leucine - metabolism</subject><subject>Mitochondria - enzymology</subject><subject>Rats</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1966</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFtLwzAYhoMocx5-wiB4IXpRTdImTS_H0CluDDyAdyFNvrpI02rSofv3dm7su3kv3sMHD0IjSm4ooeL2hRBGk4JxeUXldSGEkIk8QENKZJqknL4fouE-coxOYvwk_WUFHaABLzIhUjpE00lYx07XtWsAz7X3una6wXUy9q5p8dg4ixe_zuoIuAqtx8-6w0_ONrDGc9e1Ztk2Njh9ho4qXUc43-kperu_e508JLPF9HEyniUmzWWXmEoaLrTOmBUGiJQCaCnSnInSSi1yMIKLqmRaECjzouS0MrzICUibcZGz9BRdbne_Qvu9gtgp76KButYNtKuoZMYoZwXvg3wbNKGNMUClvoLzOqwVJWoDUP0DVBs6ikr1D1DJvjfaPViVHuy-tSPW-xdbf-k-lj8ugCpdTwG8Ylm_phjJefoH9k92tw</recordid><startdate>19660510</startdate><enddate>19660510</enddate><creator>Nakano, M</creator><creator>Danowski, T S</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>7X8</scope></search><sort><creationdate>19660510</creationdate><title>Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria</title><author>Nakano, M ; Danowski, T S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-cf8c56aa42d6ce0886e1b63726bd8a67ec656fb2a60eb79b51fc5970e8d456723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1966</creationdate><topic>Amino Acid Oxidoreductases - metabolism</topic><topic>Animals</topic><topic>Chemistry Techniques, Analytical</topic><topic>Chromatography, Gel</topic><topic>Crystallization</topic><topic>Electrophoresis</topic><topic>Flavin Mononucleotide</topic><topic>Glycine - metabolism</topic><topic>Hydroxybutyrates - metabolism</topic><topic>In Vitro Techniques</topic><topic>Kidney - cytology</topic><topic>Kidney - enzymology</topic><topic>Lactates - metabolism</topic><topic>Leucine - metabolism</topic><topic>Mitochondria - enzymology</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakano, M</creatorcontrib><creatorcontrib>Danowski, T S</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakano, M</au><au>Danowski, T S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1966-05-10</date><risdate>1966</risdate><volume>241</volume><issue>9</issue><spage>2075</spage><epage>2083</epage><pages>2075-2083</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>l -Amino acid oxidase has been crystallized from extracts of rat kidney mitochondria. Purification involved sonic extraction,
ammonium sulfate fractionation, chromatography on diethylaminoethyl cellulose, and gel filtration through Sephadex G-200.
The enzyme revealed a single protein band on starch gel electrophoresis and exhibited a single homogeneous peak ( s 20, w 0 = 10.5 S) in an ultracentrifuge.
The enzyme is a flavoprotein in which the prosthetic group appears to be flavin mononucleotide. On the basis of the flavin
mononucleotide content of the enzyme (0.92%) and its molecular weight (88,900 ± 1,100), it has been concluded that the enzyme
contains 2 moles of flavin mononucleotide per mole.
The enzyme catalyzes the oxidation of many α-aminomonocarboxylic and α-hydroxy acids ( l configuration) but has no action on optically inactive acids such as glycine and α-hydroxyisobutyric acid. The turnover numbers
for the oxidation of l -leucine and of l -lactic acid were 6.3 and 26 moles per min per mole of flavin mononucleotide conjugated with enzyme, respectively.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>5946631</pmid><doi>10.1016/S0021-9258(18)96668-8</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1966-05, Vol.241 (9), p.2075-2083 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Oxidoreductases - metabolism Animals Chemistry Techniques, Analytical Chromatography, Gel Crystallization Electrophoresis Flavin Mononucleotide Glycine - metabolism Hydroxybutyrates - metabolism In Vitro Techniques Kidney - cytology Kidney - enzymology Lactates - metabolism Leucine - metabolism Mitochondria - enzymology Rats |
| title | Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria |
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