Serveur d'exploration sur le cobalt au Maghreb

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<title xml:lang="en">Proteolytic activities in
<italic>Phaseolus vulgaris</italic>
cotyledons under copper stress</title>
<author>
<name sortKey="Karmous, Ines" sort="Karmous, Ines" uniqKey="Karmous I" first="Inès" last="Karmous">Inès Karmous</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
</affiliation>
</author>
<author>
<name sortKey="Khadija, Jaouani" sort="Khadija, Jaouani" uniqKey="Khadija J" first="Jaouani" last="Khadija">Jaouani Khadija</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
</affiliation>
</author>
<author>
<name sortKey="Chaoui, Abdelilah" sort="Chaoui, Abdelilah" uniqKey="Chaoui A" first="Abdelilah" last="Chaoui">Abdelilah Chaoui</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
</affiliation>
</author>
<author>
<name sortKey="El Ferjani, Ezzedine" sort="El Ferjani, Ezzedine" uniqKey="El Ferjani E" first="Ezzedine" last="El Ferjani">Ezzedine El Ferjani</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
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<date when="2012">2012</date>
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<title xml:lang="en" level="a" type="main">Proteolytic activities in
<italic>Phaseolus vulgaris</italic>
cotyledons under copper stress</title>
<author>
<name sortKey="Karmous, Ines" sort="Karmous, Ines" uniqKey="Karmous I" first="Inès" last="Karmous">Inès Karmous</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
</affiliation>
</author>
<author>
<name sortKey="Khadija, Jaouani" sort="Khadija, Jaouani" uniqKey="Khadija J" first="Jaouani" last="Khadija">Jaouani Khadija</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
</affiliation>
</author>
<author>
<name sortKey="Chaoui, Abdelilah" sort="Chaoui, Abdelilah" uniqKey="Chaoui A" first="Abdelilah" last="Chaoui">Abdelilah Chaoui</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
</affiliation>
</author>
<author>
<name sortKey="El Ferjani, Ezzedine" sort="El Ferjani, Ezzedine" uniqKey="El Ferjani E" first="Ezzedine" last="El Ferjani">Ezzedine El Ferjani</name>
<affiliation>
<nlm:aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</nlm:aff>
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</author>
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<series>
<title level="j">Physiology and Molecular Biology of Plants</title>
<idno type="ISSN">0971-5894</idno>
<idno type="eISSN">0974-0430</idno>
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<date when="2012">2012</date>
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<p>The changes in the protease activities of bean cotyledons were investigated in response to copper stress. Assays using synthetic substrates and specific protease inhibitors followed by activity measurements and electrophoresis analysis allowed to study the classes of enzymes involved in the storage protein mobilization during the germination of bean (
<italic>Phaseolus vulgaris</italic>
L) seeds, and then identify which ones were affected in the presence of 200 μM CuCl
<sub>2</sub>
in the imbibition medium. Copper treatment affected embryo growth and total protease activity. The results of SDS-gelatin-PAGE show that Cu excess led to a decrease in protease activity of 45 to 66 kDa. Moreover, cysteine-, aspartic- and metallo-protease activities were markedly lowered under copper stress, while serine-protease one was enhanced as well as its activity dependent abundance in comparison with control. However, the relative distribution of major cysteine protease in H
<sub>2</sub>
O-germinated seeds was significantly diminished after Cu exposure. Thus, copper excess can disturb the nitrogen freeing from reserve tissues at enzymatic level; differential responses of protease classes are discussed, notably, cysteine protease in the way of storage protein mobilization and serine protease in protective mechanism one.</p>
</div>
</front>
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<pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Physiol Mol Biol Plants</journal-id>
<journal-id journal-id-type="iso-abbrev">Physiol Mol Biol Plants</journal-id>
<journal-title-group>
<journal-title>Physiology and Molecular Biology of Plants</journal-title>
</journal-title-group>
<issn pub-type="ppub">0971-5894</issn>
<issn pub-type="epub">0974-0430</issn>
<publisher>
<publisher-name>Springer India</publisher-name>
<publisher-loc>New Delhi</publisher-loc>
</publisher>
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<article-meta>
<article-id pub-id-type="pmid">24082496</article-id>
<article-id pub-id-type="pmc">3550548</article-id>
<article-id pub-id-type="publisher-id">128</article-id>
<article-id pub-id-type="doi">10.1007/s12298-012-0128-4</article-id>
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<subj-group subj-group-type="heading">
<subject>Research Article</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Proteolytic activities in
<italic>Phaseolus vulgaris</italic>
cotyledons under copper stress</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Karmous</surname>
<given-names>Inès</given-names>
</name>
<address>
<email>ines.karmous@yahoo.fr</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Khadija</surname>
<given-names>Jaouani</given-names>
</name>
<address>
<email>j.dayja@yahoo.fr</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author" corresp="yes">
<name>
<surname>Chaoui</surname>
<given-names>Abdelilah</given-names>
</name>
<address>
<phone>+216-72-591906</phone>
<fax>+216-72-590566</fax>
<email>cabdelilah1@yahoo.fr</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>El Ferjani</surname>
<given-names>Ezzedine</given-names>
</name>
<address>
<email>ezzferjani2002@yahoo.fr</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1">Département des Sciences de la Vie, Faculté des Sciences de Bizerte, Bio-Physiologie Cellulaires, Zarzouna, 7021 Tunisie</aff>
</contrib-group>
<pub-date pub-type="epub">
<day>12</day>
<month>8</month>
<year>2012</year>
</pub-date>
<pub-date pub-type="ppub">
<month>10</month>
<year>2012</year>
</pub-date>
<volume>18</volume>
<issue>4</issue>
<fpage>337</fpage>
<lpage>343</lpage>
<permissions>
<copyright-statement>© Prof. H.S. Srivastava Foundation for Science and Society 2012</copyright-statement>
</permissions>
<abstract id="Abs1">
<p>The changes in the protease activities of bean cotyledons were investigated in response to copper stress. Assays using synthetic substrates and specific protease inhibitors followed by activity measurements and electrophoresis analysis allowed to study the classes of enzymes involved in the storage protein mobilization during the germination of bean (
<italic>Phaseolus vulgaris</italic>
L) seeds, and then identify which ones were affected in the presence of 200 μM CuCl
<sub>2</sub>
in the imbibition medium. Copper treatment affected embryo growth and total protease activity. The results of SDS-gelatin-PAGE show that Cu excess led to a decrease in protease activity of 45 to 66 kDa. Moreover, cysteine-, aspartic- and metallo-protease activities were markedly lowered under copper stress, while serine-protease one was enhanced as well as its activity dependent abundance in comparison with control. However, the relative distribution of major cysteine protease in H
<sub>2</sub>
O-germinated seeds was significantly diminished after Cu exposure. Thus, copper excess can disturb the nitrogen freeing from reserve tissues at enzymatic level; differential responses of protease classes are discussed, notably, cysteine protease in the way of storage protein mobilization and serine protease in protective mechanism one.</p>
</abstract>
<kwd-group xml:lang="en">
<title>Keywords</title>
<kwd>Bean</kwd>
<kwd>Copper</kwd>
<kwd>Cotyledon</kwd>
<kwd>Endoprotease</kwd>
<kwd>Germination</kwd>
</kwd-group>
<custom-meta-group>
<custom-meta>
<meta-name>issue-copyright-statement</meta-name>
<meta-value>© Prof. H.S. Srivastava Foundation for Science and Society 2012</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
</pmc>
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