Molecular cloning, characterization of CAT, and eco-toxicological effects of dietary zinc oxide on antioxidant enzymes in Eisenia fetida
The full-length cDNA of catalase ( Ef CAT) from Eisenia fetida was cloned (GenBank accession no. JN617999). Sequence characterization revealed that Ef CAT protein sequence contained proximal heme-ligand signature sequence ( 351 RLFSYSDTH 359 ), two glycosylation sites (N 145 and N 436 ), the proxima...
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| creator | Xiong, Wenguang Sun, Yongxue Zou, Mengjia Muhammad, Rizwan-Ul-Haq |
| description | The full-length cDNA of catalase (
Ef
CAT) from
Eisenia fetida
was cloned (GenBank accession no. JN617999). Sequence characterization revealed that
Ef
CAT protein sequence contained proximal heme-ligand signature sequence (
351
RLFSYSDTH
359
), two glycosylation sites (N
145
and N
436
), the proximal active site signature (
61
FDRERIPERVVHAKGAGA
78
), and 12 amino acids (N
145
, H
191
, F
195
, S
198
, R
200
, N
210
, Y
212
, K
234
, I
299
, W
300
, Q
302
, and Y
355
), which were identified as putative residues involved in NADPH binding. These conserved motifs and catalase signature sequences were essential for the structure and function of
Ef
CAT. The present study also investigated the effect of the veterinary food additive zinc oxide on antioxidant processes in
E
.
fetida
, at different concentrations and exposure durations. A significant increase (by 106.0 % compared to controls) in CAT activity at 500 mg/kg was registered at day 15. The superoxide dismutase (SOD) activity at 500 mg/kg increased to the maximum value (by 44.0 %) measured at day 15. There was a significant increase in glutathione peroxidase (GPx) activity for all concentrations after 5 days. The results showed that dietary Zn (500 mg/kg) causes oxidative damage to earthworms. At early stages of earthworms exposed to ZnO, GPx is the main enzyme to impair the oxidative status; while at later stages the enzymes CAT and SOD were the main indicators of oxidative stress. The antioxidant enzymatic variations may be an adaptive response of earthworms to survive in contaminated soils. |
| doi_str_mv | 10.1007/s11356-012-1408-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1492637645</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1492637645</sourcerecordid><originalsourceid>FETCH-LOGICAL-c442t-66092836217993884baa590e50258ab59527484393caa681816ca968805826683</originalsourceid><addsrcrecordid>eNp1kc1uEzEUhS1ERUPgAdggS2xY1MV_47GXVVR-pFbdlLV149wJriZ2sWekNk_AY-OQghASqyvrfufYPoeQN4KfC877D1UI1RnGhWRCc8vcM7IQRmjWa-eekwV3WjOhtD4lL2u941xyJ_sX5FQqaVRv5IL8uM4jhnmEQsOYU0zbMxq-QYEwYYl7mGJONA90dXF7RiFtKIbMpvwQQx7zNgYYKQ4DhqkeqE3ECcoj3ccUaIM2SJscUnNphzYppv3jDiuNiV7GiikCHXBqu1fkZICx4uunuSRfP17erj6zq5tPX1YXVyxoLSdmTPuCVUaK3jllrV4DdI5jx2VnYd25TvbaauVUADBWWGECOGMt76w0xqoleX_0vS_5-4x18rtYA44jJMxz9UK7X9norqHv_kHv8lxSe50XiivZ0mxjScSRCiXXWnDw9yXuWgpecH-oyR9r8q0mf6jJu6Z5--Q8r3e4-aP43UsD5BGobZW2WP66-r-uPwErvZvZ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1303220930</pqid></control><display><type>article</type><title>Molecular cloning, characterization of CAT, and eco-toxicological effects of dietary zinc oxide on antioxidant enzymes in Eisenia fetida</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Xiong, Wenguang ; Sun, Yongxue ; Zou, Mengjia ; Muhammad, Rizwan-Ul-Haq</creator><creatorcontrib>Xiong, Wenguang ; Sun, Yongxue ; Zou, Mengjia ; Muhammad, Rizwan-Ul-Haq</creatorcontrib><description>The full-length cDNA of catalase (
Ef
CAT) from
Eisenia fetida
was cloned (GenBank accession no. JN617999). Sequence characterization revealed that
Ef
CAT protein sequence contained proximal heme-ligand signature sequence (
351
RLFSYSDTH
359
), two glycosylation sites (N
145
and N
436
), the proximal active site signature (
61
FDRERIPERVVHAKGAGA
78
), and 12 amino acids (N
145
, H
191
, F
195
, S
198
, R
200
, N
210
, Y
212
, K
234
, I
299
, W
300
, Q
302
, and Y
355
), which were identified as putative residues involved in NADPH binding. These conserved motifs and catalase signature sequences were essential for the structure and function of
Ef
CAT. The present study also investigated the effect of the veterinary food additive zinc oxide on antioxidant processes in
E
.
fetida
, at different concentrations and exposure durations. A significant increase (by 106.0 % compared to controls) in CAT activity at 500 mg/kg was registered at day 15. The superoxide dismutase (SOD) activity at 500 mg/kg increased to the maximum value (by 44.0 %) measured at day 15. There was a significant increase in glutathione peroxidase (GPx) activity for all concentrations after 5 days. The results showed that dietary Zn (500 mg/kg) causes oxidative damage to earthworms. At early stages of earthworms exposed to ZnO, GPx is the main enzyme to impair the oxidative status; while at later stages the enzymes CAT and SOD were the main indicators of oxidative stress. The antioxidant enzymatic variations may be an adaptive response of earthworms to survive in contaminated soils.</description><identifier>ISSN: 0944-1344</identifier><identifier>EISSN: 1614-7499</identifier><identifier>DOI: 10.1007/s11356-012-1408-9</identifier><identifier>PMID: 23263762</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Antioxidants ; Aquatic Pollution ; Atmospheric Protection/Air Quality Control/Air Pollution ; Biomarkers ; Catalase ; Catalase - genetics ; Catalytic Domain - genetics ; Cloning ; Earth and Environmental Science ; Ecotoxicology ; Eisenia fetida ; Environment ; Environmental Chemistry ; Environmental Health ; Environmental science ; Enzymes ; Food additives ; Food processing ; Glutathione peroxidase ; Glutathione Peroxidase - drug effects ; Glutathione Peroxidase - metabolism ; Glycosylation ; Investigations ; Laboratories ; Malondialdehyde - analysis ; Molecular Sequence Data ; Nitrogen ; Oligochaeta ; Oligochaeta - chemistry ; Oligochaeta - drug effects ; Oligochaeta - enzymology ; Oligochaeta - genetics ; Oxidation-Reduction - drug effects ; Oxidative stress ; Oxidative Stress - drug effects ; Phylogeny ; Potassium ; Research Article ; Sequence Alignment ; Soil contamination ; Soil Pollutants - toxicity ; Soil pollution ; Structure-function relationships ; Studies ; Superoxide dismutase ; Superoxide Dismutase - drug effects ; Superoxide Dismutase - metabolism ; Veterinary medicine ; Waste Water Technology ; Water Management ; Water Pollution Control ; Worms ; Zinc oxide ; Zinc Oxide - pharmacology ; Zinc oxides</subject><ispartof>Environmental science and pollution research international, 2013-03, Vol.20 (3), p.1746-1755</ispartof><rights>Springer-Verlag Berlin Heidelberg 2012</rights><rights>Springer-Verlag Berlin Heidelberg 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-66092836217993884baa590e50258ab59527484393caa681816ca968805826683</citedby><cites>FETCH-LOGICAL-c442t-66092836217993884baa590e50258ab59527484393caa681816ca968805826683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11356-012-1408-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11356-012-1408-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27922,27923,41486,42555,51317</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23263762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xiong, Wenguang</creatorcontrib><creatorcontrib>Sun, Yongxue</creatorcontrib><creatorcontrib>Zou, Mengjia</creatorcontrib><creatorcontrib>Muhammad, Rizwan-Ul-Haq</creatorcontrib><title>Molecular cloning, characterization of CAT, and eco-toxicological effects of dietary zinc oxide on antioxidant enzymes in Eisenia fetida</title><title>Environmental science and pollution research international</title><addtitle>Environ Sci Pollut Res</addtitle><addtitle>Environ Sci Pollut Res Int</addtitle><description>The full-length cDNA of catalase (
Ef
CAT) from
Eisenia fetida
was cloned (GenBank accession no. JN617999). Sequence characterization revealed that
Ef
CAT protein sequence contained proximal heme-ligand signature sequence (
351
RLFSYSDTH
359
), two glycosylation sites (N
145
and N
436
), the proximal active site signature (
61
FDRERIPERVVHAKGAGA
78
), and 12 amino acids (N
145
, H
191
, F
195
, S
198
, R
200
, N
210
, Y
212
, K
234
, I
299
, W
300
, Q
302
, and Y
355
), which were identified as putative residues involved in NADPH binding. These conserved motifs and catalase signature sequences were essential for the structure and function of
Ef
CAT. The present study also investigated the effect of the veterinary food additive zinc oxide on antioxidant processes in
E
.
fetida
, at different concentrations and exposure durations. A significant increase (by 106.0 % compared to controls) in CAT activity at 500 mg/kg was registered at day 15. The superoxide dismutase (SOD) activity at 500 mg/kg increased to the maximum value (by 44.0 %) measured at day 15. There was a significant increase in glutathione peroxidase (GPx) activity for all concentrations after 5 days. The results showed that dietary Zn (500 mg/kg) causes oxidative damage to earthworms. At early stages of earthworms exposed to ZnO, GPx is the main enzyme to impair the oxidative status; while at later stages the enzymes CAT and SOD were the main indicators of oxidative stress. The antioxidant enzymatic variations may be an adaptive response of earthworms to survive in contaminated soils.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antioxidants</subject><subject>Aquatic Pollution</subject><subject>Atmospheric Protection/Air Quality Control/Air Pollution</subject><subject>Biomarkers</subject><subject>Catalase</subject><subject>Catalase - genetics</subject><subject>Catalytic Domain - genetics</subject><subject>Cloning</subject><subject>Earth and Environmental Science</subject><subject>Ecotoxicology</subject><subject>Eisenia fetida</subject><subject>Environment</subject><subject>Environmental Chemistry</subject><subject>Environmental Health</subject><subject>Environmental science</subject><subject>Enzymes</subject><subject>Food additives</subject><subject>Food processing</subject><subject>Glutathione peroxidase</subject><subject>Glutathione Peroxidase - drug effects</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Glycosylation</subject><subject>Investigations</subject><subject>Laboratories</subject><subject>Malondialdehyde - analysis</subject><subject>Molecular Sequence Data</subject><subject>Nitrogen</subject><subject>Oligochaeta</subject><subject>Oligochaeta - chemistry</subject><subject>Oligochaeta - drug effects</subject><subject>Oligochaeta - enzymology</subject><subject>Oligochaeta - genetics</subject><subject>Oxidation-Reduction - drug effects</subject><subject>Oxidative stress</subject><subject>Oxidative Stress - drug effects</subject><subject>Phylogeny</subject><subject>Potassium</subject><subject>Research Article</subject><subject>Sequence Alignment</subject><subject>Soil contamination</subject><subject>Soil Pollutants - toxicity</subject><subject>Soil pollution</subject><subject>Structure-function relationships</subject><subject>Studies</subject><subject>Superoxide dismutase</subject><subject>Superoxide Dismutase - drug effects</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Veterinary medicine</subject><subject>Waste Water Technology</subject><subject>Water Management</subject><subject>Water Pollution Control</subject><subject>Worms</subject><subject>Zinc oxide</subject><subject>Zinc Oxide - pharmacology</subject><subject>Zinc oxides</subject><issn>0944-1344</issn><issn>1614-7499</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kc1uEzEUhS1ERUPgAdggS2xY1MV_47GXVVR-pFbdlLV149wJriZ2sWekNk_AY-OQghASqyvrfufYPoeQN4KfC877D1UI1RnGhWRCc8vcM7IQRmjWa-eekwV3WjOhtD4lL2u941xyJ_sX5FQqaVRv5IL8uM4jhnmEQsOYU0zbMxq-QYEwYYl7mGJONA90dXF7RiFtKIbMpvwQQx7zNgYYKQ4DhqkeqE3ECcoj3ccUaIM2SJscUnNphzYppv3jDiuNiV7GiikCHXBqu1fkZICx4uunuSRfP17erj6zq5tPX1YXVyxoLSdmTPuCVUaK3jllrV4DdI5jx2VnYd25TvbaauVUADBWWGECOGMt76w0xqoleX_0vS_5-4x18rtYA44jJMxz9UK7X9norqHv_kHv8lxSe50XiivZ0mxjScSRCiXXWnDw9yXuWgpecH-oyR9r8q0mf6jJu6Z5--Q8r3e4-aP43UsD5BGobZW2WP66-r-uPwErvZvZ</recordid><startdate>20130301</startdate><enddate>20130301</enddate><creator>Xiong, Wenguang</creator><creator>Sun, Yongxue</creator><creator>Zou, Mengjia</creator><creator>Muhammad, Rizwan-Ul-Haq</creator><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7SN</scope><scope>7T7</scope><scope>7TV</scope><scope>7U7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>P64</scope><scope>PATMY</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>7ST</scope><scope>SOI</scope></search><sort><creationdate>20130301</creationdate><title>Molecular cloning, characterization of CAT, and eco-toxicological effects of dietary zinc oxide on antioxidant enzymes in Eisenia fetida</title><author>Xiong, Wenguang ; Sun, Yongxue ; Zou, Mengjia ; Muhammad, Rizwan-Ul-Haq</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-66092836217993884baa590e50258ab59527484393caa681816ca968805826683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antioxidants</topic><topic>Aquatic Pollution</topic><topic>Atmospheric Protection/Air Quality Control/Air Pollution</topic><topic>Biomarkers</topic><topic>Catalase</topic><topic>Catalase - genetics</topic><topic>Catalytic Domain - genetics</topic><topic>Cloning</topic><topic>Earth and Environmental Science</topic><topic>Ecotoxicology</topic><topic>Eisenia fetida</topic><topic>Environment</topic><topic>Environmental Chemistry</topic><topic>Environmental Health</topic><topic>Environmental science</topic><topic>Enzymes</topic><topic>Food additives</topic><topic>Food processing</topic><topic>Glutathione peroxidase</topic><topic>Glutathione Peroxidase - drug effects</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Glycosylation</topic><topic>Investigations</topic><topic>Laboratories</topic><topic>Malondialdehyde - analysis</topic><topic>Molecular Sequence Data</topic><topic>Nitrogen</topic><topic>Oligochaeta</topic><topic>Oligochaeta - chemistry</topic><topic>Oligochaeta - drug effects</topic><topic>Oligochaeta - enzymology</topic><topic>Oligochaeta - genetics</topic><topic>Oxidation-Reduction - drug effects</topic><topic>Oxidative stress</topic><topic>Oxidative Stress - drug effects</topic><topic>Phylogeny</topic><topic>Potassium</topic><topic>Research Article</topic><topic>Sequence Alignment</topic><topic>Soil contamination</topic><topic>Soil Pollutants - toxicity</topic><topic>Soil pollution</topic><topic>Structure-function relationships</topic><topic>Studies</topic><topic>Superoxide dismutase</topic><topic>Superoxide Dismutase - drug effects</topic><topic>Superoxide Dismutase - metabolism</topic><topic>Veterinary medicine</topic><topic>Waste Water Technology</topic><topic>Water Management</topic><topic>Water Pollution Control</topic><topic>Worms</topic><topic>Zinc oxide</topic><topic>Zinc Oxide - pharmacology</topic><topic>Zinc oxides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xiong, Wenguang</creatorcontrib><creatorcontrib>Sun, Yongxue</creatorcontrib><creatorcontrib>Zou, Mengjia</creatorcontrib><creatorcontrib>Muhammad, Rizwan-Ul-Haq</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central 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(Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Environment Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Environmental science and pollution research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xiong, Wenguang</au><au>Sun, Yongxue</au><au>Zou, Mengjia</au><au>Muhammad, Rizwan-Ul-Haq</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning, characterization of CAT, and eco-toxicological effects of dietary zinc oxide on antioxidant enzymes in Eisenia fetida</atitle><jtitle>Environmental science and pollution research international</jtitle><stitle>Environ Sci Pollut Res</stitle><addtitle>Environ Sci Pollut Res Int</addtitle><date>2013-03-01</date><risdate>2013</risdate><volume>20</volume><issue>3</issue><spage>1746</spage><epage>1755</epage><pages>1746-1755</pages><issn>0944-1344</issn><eissn>1614-7499</eissn><abstract>The full-length cDNA of catalase (
Ef
CAT) from
Eisenia fetida
was cloned (GenBank accession no. JN617999). Sequence characterization revealed that
Ef
CAT protein sequence contained proximal heme-ligand signature sequence (
351
RLFSYSDTH
359
), two glycosylation sites (N
145
and N
436
), the proximal active site signature (
61
FDRERIPERVVHAKGAGA
78
), and 12 amino acids (N
145
, H
191
, F
195
, S
198
, R
200
, N
210
, Y
212
, K
234
, I
299
, W
300
, Q
302
, and Y
355
), which were identified as putative residues involved in NADPH binding. These conserved motifs and catalase signature sequences were essential for the structure and function of
Ef
CAT. The present study also investigated the effect of the veterinary food additive zinc oxide on antioxidant processes in
E
.
fetida
, at different concentrations and exposure durations. A significant increase (by 106.0 % compared to controls) in CAT activity at 500 mg/kg was registered at day 15. The superoxide dismutase (SOD) activity at 500 mg/kg increased to the maximum value (by 44.0 %) measured at day 15. There was a significant increase in glutathione peroxidase (GPx) activity for all concentrations after 5 days. The results showed that dietary Zn (500 mg/kg) causes oxidative damage to earthworms. At early stages of earthworms exposed to ZnO, GPx is the main enzyme to impair the oxidative status; while at later stages the enzymes CAT and SOD were the main indicators of oxidative stress. The antioxidant enzymatic variations may be an adaptive response of earthworms to survive in contaminated soils.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>23263762</pmid><doi>10.1007/s11356-012-1408-9</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0944-1344 |
| ispartof | Environmental science and pollution research international, 2013-03, Vol.20 (3), p.1746-1755 |
| issn | 0944-1344 1614-7499 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1492637645 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Amino acids Animals Antioxidants Aquatic Pollution Atmospheric Protection/Air Quality Control/Air Pollution Biomarkers Catalase Catalase - genetics Catalytic Domain - genetics Cloning Earth and Environmental Science Ecotoxicology Eisenia fetida Environment Environmental Chemistry Environmental Health Environmental science Enzymes Food additives Food processing Glutathione peroxidase Glutathione Peroxidase - drug effects Glutathione Peroxidase - metabolism Glycosylation Investigations Laboratories Malondialdehyde - analysis Molecular Sequence Data Nitrogen Oligochaeta Oligochaeta - chemistry Oligochaeta - drug effects Oligochaeta - enzymology Oligochaeta - genetics Oxidation-Reduction - drug effects Oxidative stress Oxidative Stress - drug effects Phylogeny Potassium Research Article Sequence Alignment Soil contamination Soil Pollutants - toxicity Soil pollution Structure-function relationships Studies Superoxide dismutase Superoxide Dismutase - drug effects Superoxide Dismutase - metabolism Veterinary medicine Waste Water Technology Water Management Water Pollution Control Worms Zinc oxide Zinc Oxide - pharmacology Zinc oxides |
| title | Molecular cloning, characterization of CAT, and eco-toxicological effects of dietary zinc oxide on antioxidant enzymes in Eisenia fetida |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T22%3A55%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Molecular%20cloning,%20characterization%20of%20CAT,%20and%20eco-toxicological%20effects%20of%20dietary%20zinc%20oxide%20on%20antioxidant%20enzymes%20in%20Eisenia%20fetida&rft.jtitle=Environmental%20science%20and%20pollution%20research%20international&rft.au=Xiong,%20Wenguang&rft.date=2013-03-01&rft.volume=20&rft.issue=3&rft.spage=1746&rft.epage=1755&rft.pages=1746-1755&rft.issn=0944-1344&rft.eissn=1614-7499&rft_id=info:doi/10.1007/s11356-012-1408-9&rft_dat=%3Cproquest_cross%3E1492637645%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1303220930&rft_id=info:pmid/23263762&rfr_iscdi=true |