Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family
Identifieur interne : 003599 ( Istex/Corpus ); précédent : 003598; suivant : 003600Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family
Auteurs : Anne M. Wang ; Yiannis A. Ioannou ; Ken M. Zeidner ; Robert J. DesnickSource :
- Molecular Genetics and Metabolism [ 1096-7192 ] ; 1998.
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Abstract
Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.
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DOI: 10.1006/mgme.1998.2750
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ISTEX:73593A7DF89C62869F91B20F5FBF4669A00C7D59Le document en format XML
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Wang</name><affiliation><mods:affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</mods:affiliation></affiliation></author><author><name sortKey="Ioannou, Yiannis A" sort="Ioannou, Yiannis A" uniqKey="Ioannou Y" first="Yiannis A." last="Ioannou">Yiannis A. Ioannou</name><affiliation><mods:affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</mods:affiliation></affiliation></author><author><name sortKey="Zeidner, Ken M" sort="Zeidner, Ken M" uniqKey="Zeidner K" first="Ken M." last="Zeidner">Ken M. Zeidner</name><affiliation><mods:affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</mods:affiliation></affiliation></author><author><name sortKey="Desnick, Robert J" sort="Desnick, Robert J" uniqKey="Desnick R" first="Robert J." last="Desnick">Robert J. Desnick</name><affiliation><mods:affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Genetics and Metabolism</title><title level="j" type="abbrev">YMGME</title><idno type="ISSN">1096-7192</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">65</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="165">165</biblScope><biblScope unit="page" to="173">173</biblScope></imprint><idno type="ISSN">1096-7192</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1096-7192</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Fabry disease</term><term>Schindler disease</term><term>cloning</term><term>gene targeting</term><term>α-N-acetylgalactosaminidase</term><term>α-galactosidase</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. 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Wang</name><affiliations><json:string>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</json:string></affiliations></json:item><json:item><name>Yiannis A. Ioannou</name><affiliations><json:string>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</json:string></affiliations></json:item><json:item><name>Ken M. Zeidner</name><affiliations><json:string>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</json:string></affiliations></json:item><json:item><name>Robert J. Desnick</name><affiliations><json:string>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>α-N-acetylgalactosaminidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>α-galactosidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cloning</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>gene targeting</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Fabry disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Schindler disease</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.</abstract><qualityIndicators><score>6.719</score><pdfVersion>1.2</pdfVersion><pdfPageSize>535 x 690 pts</pdfPageSize><refBibsNative>false</refBibsNative><keywordCount>6</keywordCount><abstractCharCount>1689</abstractCharCount><pdfWordCount>3791</pdfWordCount><pdfCharCount>25521</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>244</abstractWordCount></qualityIndicators><title>Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family</title><pii><json:string>S1096-7192(98)92750-0</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Molecular Genetics and Metabolism</title><language><json:string>unknown</json:string></language><publicationDate>1998</publicationDate><issn><json:string>1096-7192</json:string></issn><pii><json:string>S1096-7192(00)X0036-4</json:string></pii><volume>65</volume><issue>2</issue><pages><first>165</first><last>173</last></pages><genre><json:string>journal</json:string></genre></host><categories><wos><json:string>science</json:string><json:string>medicine, research & experimental</json:string><json:string>genetics & heredity</json:string><json:string>biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>biomedical research</json:string><json:string>genetics & heredity</json:string></scienceMetrix><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1998</publicationDate><copyrightDate>1998</copyrightDate><doi><json:string>10.1006/mgme.1998.2750</json:string></doi><id>73593A7DF89C62869F91B20F5FBF4669A00C7D59</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/73593A7DF89C62869F91B20F5FBF4669A00C7D59/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/73593A7DF89C62869F91B20F5FBF4669A00C7D59/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/73593A7DF89C62869F91B20F5FBF4669A00C7D59/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>©1998 Academic Press</p></availability><date>1998</date></publicationStmt><notesStmt><note type="content">Section title: Regular Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family</title><author xml:id="author-0000"><persName><forename type="first">Anne M.</forename><surname>Wang</surname></persName><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Yiannis A.</forename><surname>Ioannou</surname></persName><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Ken M.</forename><surname>Zeidner</surname></persName><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Robert J.</forename><surname>Desnick</surname></persName><affiliation>To whom correspondence should be addressed at Department of Human Genetics, Mount Sinai School of Medicine, Fifth Avenue at 100th Street, New York, NY 10029. Fax: (212) 360-1809. E-mail:rjdesnick@vaxa.crc.mssm.edu.</affiliation><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation></author><idno type="istex">73593A7DF89C62869F91B20F5FBF4669A00C7D59</idno><idno type="DOI">10.1006/mgme.1998.2750</idno><idno type="PII">S1096-7192(98)92750-0</idno></analytic><monogr><title level="j">Molecular Genetics and Metabolism</title><title level="j" type="abbrev">YMGME</title><idno type="pISSN">1096-7192</idno><idno type="PII">S1096-7192(00)X0036-4</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">65</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="165">165</biblScope><biblScope unit="page" to="173">173</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>α-N-acetylgalactosaminidase</term></item><item><term>α-galactosidase</term></item><item><term>cloning</term></item><item><term>gene targeting</term></item><item><term>Fabry disease</term></item><item><term>Schindler disease</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/73593A7DF89C62869F91B20F5FBF4669A00C7D59/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier converted-article found"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YMGME</jid><aid>92750</aid><ce:pii>S1096-7192(98)92750-0</ce:pii><ce:doi>10.1006/mgme.1998.2750</ce:doi><ce:copyright type="full-transfer" year="1998">Academic Press</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Murine α-<ce:italic>N</ce:italic>-Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family</ce:title><ce:author-group><ce:author><ce:given-name>Anne M.</ce:given-name><ce:surname>Wang</ce:surname></ce:author><ce:author><ce:given-name>Yiannis A.</ce:given-name><ce:surname>Ioannou</ce:surname></ce:author><ce:author><ce:given-name>Ken M.</ce:given-name><ce:surname>Zeidner</ce:surname></ce:author><ce:author><ce:given-name>Robert J.</ce:given-name><ce:surname>Desnick</ce:surname><ce:cross-ref refid="GM982750FN1">1</ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</ce:textfn></ce:affiliation><ce:footnote id="GM982750FN1"><ce:label>1</ce:label><ce:note-para>To whom correspondence should be addressed at Department of Human Genetics, Mount Sinai School of Medicine, Fifth Avenue at 100th Street, New York, NY 10029. Fax: (212) 360-1809. E-mail:rjdesnick@vaxa.crc.mssm.edu.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="22" month="7" year="1998"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-<ce:italic>N</ce:italic>-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>α-<ce:italic>N</ce:italic>-acetylgalactosaminidase</ce:text></ce:keyword><ce:keyword><ce:text>α-galactosidase</ce:text></ce:keyword><ce:keyword><ce:text>cloning</ce:text></ce:keyword><ce:keyword><ce:text>gene targeting</ce:text></ce:keyword><ce:keyword><ce:text>Fabry disease</ce:text></ce:keyword><ce:keyword><ce:text>Schindler disease</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Murine α-</title></titleInfo><name type="personal"><namePart type="given">Anne M.</namePart><namePart type="family">Wang</namePart><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yiannis A.</namePart><namePart type="family">Ioannou</namePart><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ken M.</namePart><namePart type="family">Zeidner</namePart><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robert J.</namePart><namePart type="family">Desnick</namePart><affiliation>Department of Human Genetics, Mount Sinai School of Medicine, New York, New York, 10029</affiliation><description>To whom correspondence should be addressed at Department of Human Genetics, Mount Sinai School of Medicine, Fifth Avenue at 100th Street, New York, NY 10029. Fax: (212) 360-1809. E-mail:rjdesnick@vaxa.crc.mssm.edu.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.</abstract><note type="content">Section title: Regular Article</note><subject lang="en"><genre>Keywords</genre><topic>α-N-acetylgalactosaminidase</topic><topic>α-galactosidase</topic><topic>cloning</topic><topic>gene targeting</topic><topic>Fabry disease</topic><topic>Schindler disease</topic></subject><relatedItem type="host"><titleInfo><title>Molecular Genetics and Metabolism</title></titleInfo><titleInfo type="abbreviated"><title>YMGME</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199810</dateIssued></originInfo><identifier type="ISSN">1096-7192</identifier><identifier type="PII">S1096-7192(00)X0036-4</identifier><part><date>199810</date><detail type="volume"><number>65</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue pages"><start>63</start><end>186</end></extent><extent unit="pages"><start>165</start><end>173</end></extent></part></relatedItem><identifier type="istex">73593A7DF89C62869F91B20F5FBF4669A00C7D59</identifier><identifier type="DOI">10.1006/mgme.1998.2750</identifier><identifier type="PII">S1096-7192(98)92750-0</identifier><accessCondition type="use and reproduction" contentType="copyright">©1998 Academic Press</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Academic Press, ©1998</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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