Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis
Identifieur interne : 005089 ( Main/Exploration ); précédent : 005088; suivant : 005090Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis
Auteurs : Luis O. Burzio [États-Unis] ; Patricio T. Riquelme [États-Unis] ; Eiji Ohtsuka [États-Unis] ; S. S. Koide [États-Unis]Source :
- 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
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 002015
- to stream Istex, to step Curation: 002015
- to stream Istex, to step Checkpoint: 002533
- to stream Main, to step Merge: 005169
- to stream Main, to step Curation: 005089
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title><author><name sortKey="Burzio, Luis O" sort="Burzio, Luis O" uniqKey="Burzio L" first="Luis O." last="Burzio">Luis O. Burzio</name></author><author><name sortKey="Riquelme, Patricio T" sort="Riquelme, Patricio T" uniqKey="Riquelme P" first="Patricio T." last="Riquelme">Patricio T. Riquelme</name></author><author><name sortKey="Ohtsuka, Eiji" sort="Ohtsuka, Eiji" uniqKey="Ohtsuka E" first="Eiji" last="Ohtsuka">Eiji Ohtsuka</name></author><author><name sortKey="Koide, S S" sort="Koide, S S" uniqKey="Koide S" first="S. S." last="Koide">S. S. Koide</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:F0C0765023672DACF9D010AA09360C136E801BA4</idno><date when="1976" year="1976">1976</date><idno type="doi">10.1016/0003-9861(76)90264-2</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-QQS32J6J-T/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">002015</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002015</idno><idno type="wicri:Area/Istex/Curation">002015</idno><idno type="wicri:Area/Istex/Checkpoint">002533</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002533</idno><idno type="wicri:doubleKey">0003-9861:1976:Burzio L:evidence:for:two</idno><idno type="wicri:Area/Main/Merge">005169</idno><idno type="wicri:Area/Main/Curation">005089</idno><idno type="wicri:Area/Main/Exploration">005089</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis</title><author><name sortKey="Burzio, Luis O" sort="Burzio, Luis O" uniqKey="Burzio L" first="Luis O." last="Burzio">Luis O. Burzio</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York</wicri:cityArea></affiliation></author><author><name sortKey="Riquelme, Patricio T" sort="Riquelme, Patricio T" uniqKey="Riquelme P" first="Patricio T." last="Riquelme">Patricio T. Riquelme</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York</wicri:cityArea></affiliation></author><author><name sortKey="Ohtsuka, Eiji" sort="Ohtsuka, Eiji" uniqKey="Ohtsuka E" first="Eiji" last="Ohtsuka">Eiji Ohtsuka</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York</wicri:cityArea></affiliation></author><author><name sortKey="Koide, S S" sort="Koide, S S" uniqKey="Koide S" first="S. S." last="Koide">S. S. Koide</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>The Population Council, The Rockefeller University, York Avenue and 66th Street, New York</wicri:cityArea></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><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Burzio, Luis O" sort="Burzio, Luis O" uniqKey="Burzio L" first="Luis O." last="Burzio">Luis O. Burzio</name></region><name sortKey="Koide, S S" sort="Koide, S S" uniqKey="Koide S" first="S. S." last="Koide">S. S. Koide</name><name sortKey="Ohtsuka, Eiji" sort="Ohtsuka, Eiji" uniqKey="Ohtsuka E" first="Eiji" last="Ohtsuka">Eiji Ohtsuka</name><name sortKey="Riquelme, Patricio T" sort="Riquelme, Patricio T" uniqKey="Riquelme P" first="Patricio T." last="Riquelme">Patricio T. Riquelme</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 005089 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 005089 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:F0C0765023672DACF9D010AA09360C136E801BA4
|texte= Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis
}}
| This area was generated with Dilib version V0.6.33. |  |