Gene Expression of D-Amino Acid Oxidase in Rabbit Kidney
Although D-amino acid oxidase (DAO) [EC 1.4.3.3] activity in rabbit kidney extract was undetectable, protein immunoreactive toward rabbit anti-pig kidney DAO antiserum and RNAs that hybridized with fragments of human and pig DAO cDNAs were detected distinctly in the rabbit kidney. A cDNA clone, RD22...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1990-09, Vol.108 (3), p.406-413 |
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| creator | Momoi, Kyoko Fukui, Kiyoshi Tada, Masazumi Miyake, Yoshihiro |
| description | Although D-amino acid oxidase (DAO) [EC 1.4.3.3] activity in rabbit kidney extract was undetectable, protein immunoreactive toward rabbit anti-pig kidney DAO antiserum and RNAs that hybridized with fragments of human and pig DAO cDNAs were detected distinctly in the rabbit kidney. A cDNA clone, RD22, was isolated from the rabbit kidney cDNA library by hybridization with a fragment of human DAO cDNA. Analysis of the nucleotide sequence revealed a 2,018 nucleotide sequence encoding a protein consisted of 347 amino acids. The number of amino acid residues was identical with those of human and pig DAOs, and the amino acid sequence showed 80 and 83% identity with pig and human DAOs, respectively. RNAs that hybridized with RD22 DNA fragment also existed in rabbit kidney, and their sizes were the same as those of the RNAs detected with the human and pig DAO cDNA fragments. RD22-derived protein was hardly synthesized by an in vitro expression system. However, a cDNA fragment lacking most of the 5′ -untranslated region and its mutants containing base changes around the initiation codon did direct protein synthesis. Moreover, the protein derived from the partial cDNA fragment containing a large part of the coding region sequence showed immunoreactivity toward anti-pig DAO antiserum. The results suggest that one of the causes of the very poor synthesis of DAO protein in rabbit kidney is translational suppression in the synthetic process. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a123214 |
| format | Article |
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A cDNA clone, RD22, was isolated from the rabbit kidney cDNA library by hybridization with a fragment of human DAO cDNA. Analysis of the nucleotide sequence revealed a 2,018 nucleotide sequence encoding a protein consisted of 347 amino acids. The number of amino acid residues was identical with those of human and pig DAOs, and the amino acid sequence showed 80 and 83% identity with pig and human DAOs, respectively. RNAs that hybridized with RD22 DNA fragment also existed in rabbit kidney, and their sizes were the same as those of the RNAs detected with the human and pig DAO cDNA fragments. RD22-derived protein was hardly synthesized by an in vitro expression system. However, a cDNA fragment lacking most of the 5′ -untranslated region and its mutants containing base changes around the initiation codon did direct protein synthesis. Moreover, the protein derived from the partial cDNA fragment containing a large part of the coding region sequence showed immunoreactivity toward anti-pig DAO antiserum. The results suggest that one of the causes of the very poor synthesis of DAO protein in rabbit kidney is translational suppression in the synthetic process.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a123214</identifier><identifier>PMID: 1980495</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Blotting, Western ; D-Amino-Acid Oxidase - biosynthesis ; D-Amino-Acid Oxidase - genetics ; DNA - chemistry ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation, Enzymologic ; Humans ; In Vitro Techniques ; Kidney - enzymology ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Mutagenesis ; Protein Biosynthesis ; Rabbits ; Restriction Mapping ; Swine</subject><ispartof>Journal of biochemistry (Tokyo), 1990-09, Vol.108 (3), p.406-413</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19326110$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1980495$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Momoi, Kyoko</creatorcontrib><creatorcontrib>Fukui, Kiyoshi</creatorcontrib><creatorcontrib>Tada, Masazumi</creatorcontrib><creatorcontrib>Miyake, Yoshihiro</creatorcontrib><title>Gene Expression of D-Amino Acid Oxidase in Rabbit Kidney</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Although D-amino acid oxidase (DAO) [EC 1.4.3.3] activity in rabbit kidney extract was undetectable, protein immunoreactive toward rabbit anti-pig kidney DAO antiserum and RNAs that hybridized with fragments of human and pig DAO cDNAs were detected distinctly in the rabbit kidney. A cDNA clone, RD22, was isolated from the rabbit kidney cDNA library by hybridization with a fragment of human DAO cDNA. Analysis of the nucleotide sequence revealed a 2,018 nucleotide sequence encoding a protein consisted of 347 amino acids. The number of amino acid residues was identical with those of human and pig DAOs, and the amino acid sequence showed 80 and 83% identity with pig and human DAOs, respectively. RNAs that hybridized with RD22 DNA fragment also existed in rabbit kidney, and their sizes were the same as those of the RNAs detected with the human and pig DAO cDNA fragments. RD22-derived protein was hardly synthesized by an in vitro expression system. However, a cDNA fragment lacking most of the 5′ -untranslated region and its mutants containing base changes around the initiation codon did direct protein synthesis. Moreover, the protein derived from the partial cDNA fragment containing a large part of the coding region sequence showed immunoreactivity toward anti-pig DAO antiserum. The results suggest that one of the causes of the very poor synthesis of DAO protein in rabbit kidney is translational suppression in the synthetic process.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>D-Amino-Acid Oxidase - biosynthesis</subject><subject>D-Amino-Acid Oxidase - genetics</subject><subject>DNA - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Kidney - enzymology</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>Protein Biosynthesis</subject><subject>Rabbits</subject><subject>Restriction Mapping</subject><subject>Swine</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNj01Lw0AQhhdRaq3-BCGXekvdj2SzOZZaW22lKCrFS5hsdnFrsqnZBNJ_b4pBPA3D8_DOOwiNCZ4QHLPbstVlle3KprKQu8kulZ-qmAChjJLgBA1JFHKf8pCcoiHGlPgxDbbn6MK53XGljA3QgMQCB3E4RGKhrPLm7b5SzpnSeqX27vxpYWzpTaXJvE1rMnDKM9Z7gTQ1tbcymVWHS3Smu_vqqp8j9HY_f50t_fVm8TCbrn3DIlH7Mo6EEoJAQFNOSMxoyDCWPIKub4wlpFIDaIUjpkFrTVIBcRZwmvFMCI3ZCN385u6r8rtRrk4K46TKc7CqbFxCOA8DEhzF615s0kJlyb4yBVSHpH-14-Oeg5OQ6wqsNO6fxmhX8Jjj_3rG1ar941B9JTxiUZgstx_J89Nqtn6fkeSR_QBruHb5</recordid><startdate>19900901</startdate><enddate>19900901</enddate><creator>Momoi, Kyoko</creator><creator>Fukui, Kiyoshi</creator><creator>Tada, Masazumi</creator><creator>Miyake, Yoshihiro</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19900901</creationdate><title>Gene Expression of D-Amino Acid Oxidase in Rabbit Kidney</title><author>Momoi, Kyoko ; Fukui, Kiyoshi ; Tada, Masazumi ; Miyake, Yoshihiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i378t-c978e881a42b6119325300c67a23290cabcfaafe073fafff1b8a9d462d6d88f03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>D-Amino-Acid Oxidase - biosynthesis</topic><topic>D-Amino-Acid Oxidase - genetics</topic><topic>DNA - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Kidney - enzymology</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>Protein Biosynthesis</topic><topic>Rabbits</topic><topic>Restriction Mapping</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Momoi, Kyoko</creatorcontrib><creatorcontrib>Fukui, Kiyoshi</creatorcontrib><creatorcontrib>Tada, Masazumi</creatorcontrib><creatorcontrib>Miyake, Yoshihiro</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Momoi, Kyoko</au><au>Fukui, Kiyoshi</au><au>Tada, Masazumi</au><au>Miyake, Yoshihiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene Expression of D-Amino Acid Oxidase in Rabbit Kidney</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1990-09-01</date><risdate>1990</risdate><volume>108</volume><issue>3</issue><spage>406</spage><epage>413</epage><pages>406-413</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Although D-amino acid oxidase (DAO) [EC 1.4.3.3] activity in rabbit kidney extract was undetectable, protein immunoreactive toward rabbit anti-pig kidney DAO antiserum and RNAs that hybridized with fragments of human and pig DAO cDNAs were detected distinctly in the rabbit kidney. A cDNA clone, RD22, was isolated from the rabbit kidney cDNA library by hybridization with a fragment of human DAO cDNA. Analysis of the nucleotide sequence revealed a 2,018 nucleotide sequence encoding a protein consisted of 347 amino acids. The number of amino acid residues was identical with those of human and pig DAOs, and the amino acid sequence showed 80 and 83% identity with pig and human DAOs, respectively. RNAs that hybridized with RD22 DNA fragment also existed in rabbit kidney, and their sizes were the same as those of the RNAs detected with the human and pig DAO cDNA fragments. RD22-derived protein was hardly synthesized by an in vitro expression system. However, a cDNA fragment lacking most of the 5′ -untranslated region and its mutants containing base changes around the initiation codon did direct protein synthesis. Moreover, the protein derived from the partial cDNA fragment containing a large part of the coding region sequence showed immunoreactivity toward anti-pig DAO antiserum. The results suggest that one of the causes of the very poor synthesis of DAO protein in rabbit kidney is translational suppression in the synthetic process.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>1980495</pmid><doi>10.1093/oxfordjournals.jbchem.a123214</doi><tpages>8</tpages></addata></record> |
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| ispartof | Journal of biochemistry (Tokyo), 1990-09, Vol.108 (3), p.406-413 |
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| source | MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry; Oxford University Press Journals Digital Archive Legacy |
| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Blotting, Western D-Amino-Acid Oxidase - biosynthesis D-Amino-Acid Oxidase - genetics DNA - chemistry Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation, Enzymologic Humans In Vitro Techniques Kidney - enzymology Molecular and cellular biology Molecular genetics Molecular Sequence Data Mutagenesis Protein Biosynthesis Rabbits Restriction Mapping Swine |
| title | Gene Expression of D-Amino Acid Oxidase in Rabbit Kidney |
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