Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis
Identifieur interne : 002015 ( Istex/Corpus ); précédent : 002014; suivant : 002016Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis
Auteurs : Luis O. Burzio ; Patricio T. Riquelme ; Eiji Ohtsuka ; S. S. KoideSource :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1976.
English descriptors
- Teeft :
- Absorbance, Academic press, Acceptor protein, Adenosine, Adenosine diphosphate ribose, Alkaline phosphatase, Assay, Average chain length, Biochem, Biol, Biophys, Burzio, Calf thymus glycohydrolase, Chem, Chromatographic procedure, Commun, Diphosphate, Diphosphate ribose, Elution position, Enzymatic activity, Enzyme, Glycohydrolase, Glycohydrolase activity, Glycohydrolases, Hayaishi, Hydrolytic, Hydrolytic activity, Immature testis, Linear gradient, Liver nuclei, Maximal activity, Methods section, Miwa, Other hand, Paper chromatography, Phosphatase, Phosphocellulose, Phosphocellulose column, Phosphodiesterase, Polymer, Potassium phosphate buffer, Reaction mixture, Reaction products, Ribose, Seminiferous tubules, Small shoulder, Soluble, Soluble fraction, Solvent system, Specific activity, Standard reaction mixture, Sugimura, Supernatant fraction, Testis, Testis glycohydrolase, Testis glycohydrolases, Thymus, Total activity, Ueda, Variant, Various tissues, Venom phosphodiesterase, Void volume.
Abstract
Abstract: The specific activity of rat poly(adenosine diphosphate ribose) glycohydrolase was higher in the testis than in the liver, brain, spleen or kidney. The enzyme was found primarily in the soluble fraction of the testis. When the soluble enzyme was chromatographed on phosphocellulose, the activity eluted in two peaks, at 0.22 and 0.34 m KCl, respectively, referred to in the present study as enzyme A and B. Enzyme A has an optimal pH of 7.25 and was stimulated by 150 mm KCl. The optimal pH of enyzme B was 6.5, but it was not stimulated by KCl. For maximal activity both enzymes required 10 mm 2-mercaptoethanol, and they were strongly inhibited by 100 μmp-chloromercuribenzoate. The Km values of enzyme A and B for poly(adenosine diphosphate ribose) were 1.52 and 0.70 μm, respectively. Ribose 5′-phosphate, guanosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate and adenosine diphosphate ribose inhibited both enzymes. The two latter nucleotides behave as noncompetitive inhibitors. Denatured DNA and the homopolypurines poly(G), poly(I) and poly(A) were very potent inhibitors of both glycohydrolases. The mode of hydrolysis of poly(adenosine diphosphate ribose) by glycohydrolases A and B was exoglycosidic, yielding adenosine diphosphate ribose as the final product.
Url:
DOI: 10.1016/0003-9861(76)90264-2
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ISTEX:F0C0765023672DACF9D010AA09360C136E801BA4Le document en format XML
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Koide</name><affiliation><mods:affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1976">1976</date><biblScope unit="volume">173</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="306">306</biblScope><biblScope unit="page" to="319">319</biblScope></imprint><idno type="ISSN">0003-9861</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Absorbance</term><term>Academic press</term><term>Acceptor protein</term><term>Adenosine</term><term>Adenosine diphosphate ribose</term><term>Alkaline phosphatase</term><term>Assay</term><term>Average chain length</term><term>Biochem</term><term>Biol</term><term>Biophys</term><term>Burzio</term><term>Calf thymus glycohydrolase</term><term>Chem</term><term>Chromatographic procedure</term><term>Commun</term><term>Diphosphate</term><term>Diphosphate ribose</term><term>Elution position</term><term>Enzymatic activity</term><term>Enzyme</term><term>Glycohydrolase</term><term>Glycohydrolase activity</term><term>Glycohydrolases</term><term>Hayaishi</term><term>Hydrolytic</term><term>Hydrolytic activity</term><term>Immature testis</term><term>Linear gradient</term><term>Liver nuclei</term><term>Maximal activity</term><term>Methods section</term><term>Miwa</term><term>Other hand</term><term>Paper chromatography</term><term>Phosphatase</term><term>Phosphocellulose</term><term>Phosphocellulose column</term><term>Phosphodiesterase</term><term>Polymer</term><term>Potassium phosphate buffer</term><term>Reaction mixture</term><term>Reaction products</term><term>Ribose</term><term>Seminiferous tubules</term><term>Small shoulder</term><term>Soluble</term><term>Soluble fraction</term><term>Solvent system</term><term>Specific activity</term><term>Standard reaction mixture</term><term>Sugimura</term><term>Supernatant fraction</term><term>Testis</term><term>Testis glycohydrolase</term><term>Testis glycohydrolases</term><term>Thymus</term><term>Total activity</term><term>Ueda</term><term>Variant</term><term>Various tissues</term><term>Venom phosphodiesterase</term><term>Void volume</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The specific activity of rat poly(adenosine diphosphate ribose) glycohydrolase was higher in the testis than in the liver, brain, spleen or kidney. The enzyme was found primarily in the soluble fraction of the testis. When the soluble enzyme was chromatographed on phosphocellulose, the activity eluted in two peaks, at 0.22 and 0.34 m KCl, respectively, referred to in the present study as enzyme A and B. Enzyme A has an optimal pH of 7.25 and was stimulated by 150 mm KCl. The optimal pH of enyzme B was 6.5, but it was not stimulated by KCl. For maximal activity both enzymes required 10 mm 2-mercaptoethanol, and they were strongly inhibited by 100 μmp-chloromercuribenzoate. The Km values of enzyme A and B for poly(adenosine diphosphate ribose) were 1.52 and 0.70 μm, respectively. Ribose 5′-phosphate, guanosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate and adenosine diphosphate ribose inhibited both enzymes. The two latter nucleotides behave as noncompetitive inhibitors. Denatured DNA and the homopolypurines poly(G), poly(I) and poly(A) were very potent inhibitors of both glycohydrolases. The mode of hydrolysis of poly(adenosine diphosphate ribose) by glycohydrolases A and B was exoglycosidic, yielding adenosine diphosphate ribose as the final product.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>glycohydrolase</json:string><json:string>testis</json:string><json:string>glycohydrolases</json:string><json:string>ribose</json:string><json:string>adenosine</json:string><json:string>phosphocellulose</json:string><json:string>biochem</json:string><json:string>diphosphate</json:string><json:string>biol</json:string><json:string>phosphodiesterase</json:string><json:string>soluble fraction</json:string><json:string>chem</json:string><json:string>biophys</json:string><json:string>polymer</json:string><json:string>sugimura</json:string><json:string>thymus</json:string><json:string>ueda</json:string><json:string>commun</json:string><json:string>reaction mixture</json:string><json:string>hayaishi</json:string><json:string>burzio</json:string><json:string>potassium phosphate buffer</json:string><json:string>phosphatase</json:string><json:string>diphosphate ribose</json:string><json:string>miwa</json:string><json:string>enzyme</json:string><json:string>venom phosphodiesterase</json:string><json:string>absorbance</json:string><json:string>hydrolytic</json:string><json:string>testis glycohydrolase</json:string><json:string>other hand</json:string><json:string>enzymatic activity</json:string><json:string>phosphocellulose column</json:string><json:string>total activity</json:string><json:string>testis glycohydrolases</json:string><json:string>reaction products</json:string><json:string>standard reaction mixture</json:string><json:string>adenosine diphosphate ribose</json:string><json:string>maximal activity</json:string><json:string>glycohydrolase activity</json:string><json:string>paper chromatography</json:string><json:string>assay</json:string><json:string>alkaline phosphatase</json:string><json:string>linear gradient</json:string><json:string>seminiferous tubules</json:string><json:string>liver nuclei</json:string><json:string>academic press</json:string><json:string>specific activity</json:string><json:string>soluble</json:string><json:string>variant</json:string><json:string>immature testis</json:string><json:string>supernatant fraction</json:string><json:string>solvent system</json:string><json:string>elution position</json:string><json:string>void volume</json:string><json:string>calf thymus glycohydrolase</json:string><json:string>acceptor protein</json:string><json:string>average chain length</json:string><json:string>chromatographic procedure</json:string><json:string>various tissues</json:string><json:string>hydrolytic activity</json:string><json:string>methods section</json:string><json:string>small shoulder</json:string></teeft></keywords><author><json:item><name>Luis O. Burzio</name><affiliations><json:string>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</json:string></affiliations></json:item><json:item><name>Patricio T. Riquelme</name><affiliations><json:string>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</json:string></affiliations></json:item><json:item><name>Eiji Ohtsuka</name><affiliations><json:string>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</json:string></affiliations></json:item><json:item><name>S.S. 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When the soluble enzyme was chromatographed on phosphocellulose, the activity eluted in two peaks, at 0.22 and 0.34 m KCl, respectively, referred to in the present study as enzyme A and B. Enzyme A has an optimal pH of 7.25 and was stimulated by 150 mm KCl. The optimal pH of enyzme B was 6.5, but it was not stimulated by KCl. For maximal activity both enzymes required 10 mm 2-mercaptoethanol, and they were strongly inhibited by 100 μmp-chloromercuribenzoate. The Km values of enzyme A and B for poly(adenosine diphosphate ribose) were 1.52 and 0.70 μm, respectively. Ribose 5′-phosphate, guanosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate and adenosine diphosphate ribose inhibited both enzymes. The two latter nucleotides behave as noncompetitive inhibitors. Denatured DNA and the homopolypurines poly(G), poly(I) and poly(A) were very potent inhibitors of both glycohydrolases. The mode of hydrolysis of poly(adenosine diphosphate ribose) by glycohydrolases A and B was exoglycosidic, yielding adenosine diphosphate ribose as the final product.</abstract><qualityIndicators><score>9.304</score><pdfWordCount>6593</pdfWordCount><pdfCharCount>43281</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>14</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>192</abstractWordCount><abstractCharCount>1288</abstractCharCount><keywordCount>1</keywordCount></qualityIndicators><title>Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title><pmid><json:string>4030</json:string></pmid><pii><json:string>0003-9861(76)90264-2</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Archives of Biochemistry and Biophysics</title><language><json:string>unknown</json:string></language><publicationDate>1976</publicationDate><issn><json:string>0003-9861</json:string></issn><pii><json:string>S0003-9861(00)X0299-8</json:string></pii><volume>173</volume><issue>1</issue><pages><first>306</first><last>319</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1780</json:string><json:string>1976</json:string></date><geogName></geogName><orgName><json:string>Biochem</json:string><json:string>Fogarty International Center Proceeding</json:string><json:string>An International Symposium</json:string><json:string>Sigma Chemical Co.</json:string><json:string>Worthington Chemical Co.</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>J. Biol</json:string><json:string>Gabriela Viz</json:string><json:string>A. Fractions</json:string><json:string>P. Rib</json:string><json:string>Previous</json:string><json:string>A. Aliquots</json:string><json:string>C. R. 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psychologie</json:string></inist></categories><publicationDate>1976</publicationDate><copyrightDate>1976</copyrightDate><doi><json:string>10.1016/0003-9861(76)90264-2</json:string></doi><id>F0C0765023672DACF9D010AA09360C136E801BA4</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QQS32J6J-T/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QQS32J6J-T/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-QQS32J6J-T/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1976</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>This work was partially supported by Research Grant No. PO1 HDO5671 HDPR from The National Institute of Child Health and Human Development.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title><author xml:id="author-0000"><persName><forename type="first">Luis O.</forename><surname>Burzio</surname></persName><note type="biography">On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</note><affiliation>On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</affiliation><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Patricio T.</forename><surname>Riquelme</surname></persName><note type="biography">On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</note><affiliation>On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</affiliation><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Eiji</forename><surname>Ohtsuka</surname></persName><note type="biography">Present Address: Department of Medicine, Yamato City Hospital, Yamato City, Kanagawa Ken, Japan.</note><affiliation>Present Address: Department of Medicine, Yamato City Hospital, Yamato City, Kanagawa Ken, Japan.</affiliation><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation></author><author xml:id="author-0003"><persName><forename type="first">S.S.</forename><surname>Koide</surname></persName><note type="biography">To whom inquiries and requests for reprints should be addressed.</note><affiliation>To whom inquiries and requests for reprints should be addressed.</affiliation><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation></author><idno type="istex">F0C0765023672DACF9D010AA09360C136E801BA4</idno><idno type="ark">ark:/67375/6H6-QQS32J6J-T</idno><idno type="DOI">10.1016/0003-9861(76)90264-2</idno><idno type="PII">0003-9861(76)90264-2</idno><idno type="article-id">76902642</idno></analytic><monogr><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="pISSN">0003-9861</idno><idno type="PII">S0003-9861(00)X0299-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1976"></date><biblScope unit="volume">173</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="306">306</biblScope><biblScope unit="page" to="319">319</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1976</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The specific activity of rat poly(adenosine diphosphate ribose) glycohydrolase was higher in the testis than in the liver, brain, spleen or kidney. The enzyme was found primarily in the soluble fraction of the testis. When the soluble enzyme was chromatographed on phosphocellulose, the activity eluted in two peaks, at 0.22 and 0.34 m KCl, respectively, referred to in the present study as enzyme A and B. Enzyme A has an optimal pH of 7.25 and was stimulated by 150 mm KCl. The optimal pH of enyzme B was 6.5, but it was not stimulated by KCl. For maximal activity both enzymes required 10 mm 2-mercaptoethanol, and they were strongly inhibited by 100 μmp-chloromercuribenzoate. The Km values of enzyme A and B for poly(adenosine diphosphate ribose) were 1.52 and 0.70 μm, respectively. Ribose 5′-phosphate, guanosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate and adenosine diphosphate ribose inhibited both enzymes. The two latter nucleotides behave as noncompetitive inhibitors. Denatured DNA and the homopolypurines poly(G), poly(I) and poly(A) were very potent inhibitors of both glycohydrolases. The mode of hydrolysis of poly(adenosine diphosphate ribose) by glycohydrolases A and B was exoglycosidic, yielding adenosine diphosphate ribose as the final product.</p></abstract><textClass><keywords scheme="keyword"><list><head>article-category</head><item><term>Biochemistry of viruses and nucleic acids</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1976">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QQS32J6J-T/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><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>YABBI</jid><aid>76902642</aid><ce:pii>0003-9861(76)90264-2</ce:pii><ce:doi>10.1016/0003-9861(76)90264-2</ce:doi><ce:copyright type="unknown" year="1976"></ce:copyright><ce:doctopics><ce:doctopic><ce:text>Biochemistry of viruses and nucleic acids</ce:text></ce:doctopic></ce:doctopics></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was partially supported by Research Grant No. PO1 HDO5671 HDPR from The National Institute of Child Health and Human Development.</ce:note-para></ce:article-footnote><ce:title>Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</ce:title><ce:author-group><ce:author><ce:given-name>Luis O.</ce:given-name><ce:surname>Burzio</ce:surname><ce:cross-ref refid="FN1"><ce:sup loc="post">2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Patricio T.</ce:given-name><ce:surname>Riquelme</ce:surname><ce:cross-ref refid="FN1"><ce:sup loc="post">2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Eiji</ce:given-name><ce:surname>Ohtsuka</ce:surname><ce:cross-ref refid="FN2"><ce:sup loc="post">3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>S.S.</ce:given-name><ce:surname>Koide</ce:surname><ce:cross-ref refid="COR1"><ce:sup loc="post">4</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>4</ce:label><ce:text>To whom inquiries and requests for reprints should be addressed.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>2</ce:label><ce:note-para>On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</ce:note-para></ce:footnote><ce:footnote id="FN2"><ce:label>3</ce:label><ce:note-para>Present Address: Department of Medicine, Yamato City Hospital, Yamato City, Kanagawa Ken, Japan.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="10" month="9" year="1975"></ce:date-received><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">The specific activity of rat poly(adenosine diphosphate ribose) glycohydrolase was higher in the testis than in the liver, brain, spleen or kidney. The enzyme was found primarily in the soluble fraction of the testis. When the soluble enzyme was chromatographed on phosphocellulose, the activity eluted in two peaks, at 0.22 and 0.34 <ce:small-caps>m</ce:small-caps> KCl, respectively, referred to in the present study as enzyme A and B. Enzyme A has an optimal pH of 7.25 and was stimulated by 150 m<ce:small-caps>m</ce:small-caps> KCl. The optimal pH of enyzme B was 6.5, but it was not stimulated by KCl. For maximal activity both enzymes required 10 m<ce:small-caps>m</ce:small-caps> 2-mercaptoethanol, and they were strongly inhibited by 100 μ<ce:small-caps>m</ce:small-caps><ce:italic>p</ce:italic>-chloromercuribenzoate. The <ce:italic>K</ce:italic><ce:inf loc="post"><ce:italic>m</ce:italic></ce:inf> values of enzyme A and B for poly(adenosine diphosphate ribose) were 1.52 and 0.70 μ<ce:small-caps>m</ce:small-caps>, respectively. Ribose 5′-phosphate, guanosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate and adenosine diphosphate ribose inhibited both enzymes. The two latter nucleotides behave as noncompetitive inhibitors. Denatured DNA and the homopolypurines poly(G), poly(I) and poly(A) were very potent inhibitors of both glycohydrolases. The mode of hydrolysis of poly(adenosine diphosphate ribose) by glycohydrolases A and B was exoglycosidic, yielding adenosine diphosphate ribose as the final product.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title></titleInfo><name type="personal"><namePart type="given">Luis O.</namePart><namePart type="family">Burzio</namePart><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation><description>On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Patricio T.</namePart><namePart type="family">Riquelme</namePart><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation><description>On leave from The Department of Biochemistry, Austral University, Valdivia, Chile.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eiji</namePart><namePart type="family">Ohtsuka</namePart><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation><description>Present Address: Department of Medicine, Yamato City Hospital, Yamato City, Kanagawa Ken, Japan.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.S.</namePart><namePart type="family">Koide</namePart><affiliation>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York, New York 10021 U.S.A.</affiliation><description>To whom inquiries and requests for reprints should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1976</dateIssued><copyrightDate encoding="w3cdtf">1976</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The specific activity of rat poly(adenosine diphosphate ribose) glycohydrolase was higher in the testis than in the liver, brain, spleen or kidney. The enzyme was found primarily in the soluble fraction of the testis. When the soluble enzyme was chromatographed on phosphocellulose, the activity eluted in two peaks, at 0.22 and 0.34 m KCl, respectively, referred to in the present study as enzyme A and B. Enzyme A has an optimal pH of 7.25 and was stimulated by 150 mm KCl. The optimal pH of enyzme B was 6.5, but it was not stimulated by KCl. For maximal activity both enzymes required 10 mm 2-mercaptoethanol, and they were strongly inhibited by 100 μmp-chloromercuribenzoate. The Km values of enzyme A and B for poly(adenosine diphosphate ribose) were 1.52 and 0.70 μm, respectively. Ribose 5′-phosphate, guanosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate and adenosine diphosphate ribose inhibited both enzymes. The two latter nucleotides behave as noncompetitive inhibitors. Denatured DNA and the homopolypurines poly(G), poly(I) and poly(A) were very potent inhibitors of both glycohydrolases. The mode of hydrolysis of poly(adenosine diphosphate ribose) by glycohydrolases A and B was exoglycosidic, yielding adenosine diphosphate ribose as the final product.</abstract><note>This work was partially supported by Research Grant No. PO1 HDO5671 HDPR from The National Institute of Child Health and Human Development.</note><subject><genre>article-category</genre><topic>Biochemistry of viruses and nucleic acids</topic></subject><relatedItem type="host"><titleInfo><title>Archives of Biochemistry and Biophysics</title></titleInfo><titleInfo type="abbreviated"><title>YABBI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1976</dateIssued></originInfo><identifier type="ISSN">0003-9861</identifier><identifier type="PII">S0003-9861(00)X0299-8</identifier><part><date>1976</date><detail type="volume"><number>173</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>393</end></extent><extent unit="pages"><start>306</start><end>319</end></extent></part></relatedItem><identifier type="istex">F0C0765023672DACF9D010AA09360C136E801BA4</identifier><identifier type="ark">ark:/67375/6H6-QQS32J6J-T</identifier><identifier type="DOI">10.1016/0003-9861(76)90264-2</identifier><identifier type="PII">0003-9861(76)90264-2</identifier><identifier type="ArticleID">76902642</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QQS32J6J-T/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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