Purification and some characteristics of chicken liver L-2-hydroxyacid oxidase A
The isozyme A of L-2-hydroxyacid oxidase is a peroxisomal flavoenzyme that catalyzes the oxidation of short-chain aliphatic L-2-hydroxyacids in many tissues of higher organisms. A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The N-terminal amino aci...
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| Veröffentlicht in: | FEBS letters 1990-06, Vol.266 (1), p.183-186 |
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| creator | Dupuis, Liliane Caro, Josiana De Brachet, Patrick Puigserver, Antoine |
| description | The isozyme A of L-2-hydroxyacid oxidase is a peroxisomal flavoenzyme that catalyzes the oxidation of short-chain aliphatic L-2-hydroxyacids in many tissues of higher organisms. A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The N-terminal amino acid of the polypeptide chain was found to be blocked as that of spinach glycolate oxidase, contrastingly with that of rat kidney isozyme B. Its amino acid composition was comparable to that of other known L-2-hydroxyacid oxidases. Despite different substrate specificity, some immunological identity was observed between chicken liver L-2-hydroxyacid isozyme A and rat kidney isozyme B. |
| doi_str_mv | 10.1016/0014-5793(90)81535-V |
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A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The N-terminal amino acid of the polypeptide chain was found to be blocked as that of spinach glycolate oxidase, contrastingly with that of rat kidney isozyme B. Its amino acid composition was comparable to that of other known L-2-hydroxyacid oxidases. Despite different substrate specificity, some immunological identity was observed between chicken liver L-2-hydroxyacid isozyme A and rat kidney isozyme B.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(90)81535-V</identifier><identifier>PMID: 2194838</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Alcohol Oxidoreductases - immunology ; Alcohol Oxidoreductases - isolation & purification ; Alcohol Oxidoreductases - metabolism ; Amino Acids - analysis ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Blotting, Western ; Chicken liver ; Chickens ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glycolate oxidase ; Isozyme A ; Kinetics ; L-2-Hydroxyacid oxidase ; liver ; Liver - enzymology ; Methionine - analogs & derivatives ; Methionine - metabolism ; Microbodies - enzymology ; Molecular Weight ; Oxidoreductases ; Peroxisome</subject><ispartof>FEBS letters, 1990-06, Vol.266 (1), p.183-186</ispartof><rights>1990</rights><rights>FEBS Letters 266 (1990) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c593V-38c80da0a08d84bab13dd0c83e8b26f60dd0e46e5c624e4dcf0f0bd04260c4da3</citedby><cites>FETCH-LOGICAL-c593V-38c80da0a08d84bab13dd0c83e8b26f60dd0e46e5c624e4dcf0f0bd04260c4da3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(90)81535-V$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19771400$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2194838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dupuis, Liliane</creatorcontrib><creatorcontrib>Caro, Josiana De</creatorcontrib><creatorcontrib>Brachet, Patrick</creatorcontrib><creatorcontrib>Puigserver, Antoine</creatorcontrib><title>Purification and some characteristics of chicken liver L-2-hydroxyacid oxidase A</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The isozyme A of L-2-hydroxyacid oxidase is a peroxisomal flavoenzyme that catalyzes the oxidation of short-chain aliphatic L-2-hydroxyacids in many tissues of higher organisms. A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The N-terminal amino acid of the polypeptide chain was found to be blocked as that of spinach glycolate oxidase, contrastingly with that of rat kidney isozyme B. Its amino acid composition was comparable to that of other known L-2-hydroxyacid oxidases. Despite different substrate specificity, some immunological identity was observed between chicken liver L-2-hydroxyacid isozyme A and rat kidney isozyme B.</description><subject>Alcohol Oxidoreductases - immunology</subject><subject>Alcohol Oxidoreductases - isolation & purification</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Amino Acids - analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Chicken liver</subject><subject>Chickens</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycolate oxidase</subject><subject>Isozyme A</subject><subject>Kinetics</subject><subject>L-2-Hydroxyacid oxidase</subject><subject>liver</subject><subject>Liver - enzymology</subject><subject>Methionine - analogs & derivatives</subject><subject>Methionine - metabolism</subject><subject>Microbodies - enzymology</subject><subject>Molecular Weight</subject><subject>Oxidoreductases</subject><subject>Peroxisome</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFv1DAQhS1EVZbCPwApFxAcAuPYTuwLUqm6tNJK9AB7tZzxRDVkk2JnS_ff43RX5QY9WfPem2f7Y-wVhw8ceP0RgMtSNUa8M_BecyVUuX7CFlw3ohSy1k_Z4iHyjD1P6QfkWXNzzI4rbqQWesGurrYxdAHdFMahcIMv0rihAq9ddDhRDGkKmIqxy1LAnzQUfbilWKzKqrze-Tje7RwGX4x3wbtExekLdtS5PtHLw3nCvi_Pv51dlKuvXy7PTlclKiPWpdCowTtwoL2WrWu58B5QC9JtVXc15IlkTQrrSpL02EEHrQdZ1YDSO3HC3u57b-L4a0tpspuQkPreDTRuk22MVjU35r9BrjKSRqkclPsgxjGlSJ29iWHj4s5ysDNxO-O0M05rwN4Tt-u89vrQv2035B-WDoiz_-bgu4Su76IbMKS_3aZpuATIueU-9zv0tHvU3XZ5_rmajVk3cK_OD_q0L6KM_zZQtAkDDUg-RMLJ-jH8-0d_AEZOsJA</recordid><startdate>19900618</startdate><enddate>19900618</enddate><creator>Dupuis, Liliane</creator><creator>Caro, Josiana De</creator><creator>Brachet, Patrick</creator><creator>Puigserver, Antoine</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900618</creationdate><title>Purification and some characteristics of chicken liver L-2-hydroxyacid oxidase A</title><author>Dupuis, Liliane ; Caro, Josiana De ; Brachet, Patrick ; Puigserver, Antoine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c593V-38c80da0a08d84bab13dd0c83e8b26f60dd0e46e5c624e4dcf0f0bd04260c4da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Alcohol Oxidoreductases - immunology</topic><topic>Alcohol Oxidoreductases - isolation & purification</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Amino Acids - analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Chicken liver</topic><topic>Chickens</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. 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A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The N-terminal amino acid of the polypeptide chain was found to be blocked as that of spinach glycolate oxidase, contrastingly with that of rat kidney isozyme B. Its amino acid composition was comparable to that of other known L-2-hydroxyacid oxidases. Despite different substrate specificity, some immunological identity was observed between chicken liver L-2-hydroxyacid isozyme A and rat kidney isozyme B.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>2194838</pmid><doi>10.1016/0014-5793(90)81535-V</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Alcohol Oxidoreductases - immunology Alcohol Oxidoreductases - isolation & purification Alcohol Oxidoreductases - metabolism Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blotting, Western Chicken liver Chickens Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glycolate oxidase Isozyme A Kinetics L-2-Hydroxyacid oxidase liver Liver - enzymology Methionine - analogs & derivatives Methionine - metabolism Microbodies - enzymology Molecular Weight Oxidoreductases Peroxisome |
| title | Purification and some characteristics of chicken liver L-2-hydroxyacid oxidase A |
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