Please use this identifier to cite or link to this item:
https://hdl.handle.net/11499/4117
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Şen, Alaattin. | - |
dc.contributor.author | Semiz, Aslı. | - |
dc.date.accessioned | 2019-08-16T11:32:18Z | |
dc.date.available | 2019-08-16T11:32:18Z | |
dc.date.issued | 2007 | - |
dc.identifier.issn | 0147-6513 | - |
dc.identifier.uri | https://hdl.handle.net/11499/4117 | - |
dc.identifier.uri | https://doi.org/10.1016/j.ecoenv.2006.08.007 | - |
dc.description.abstract | In this study, feral leaping mullet (Liza saliens) liver microsomal 7-ethoxyresorufin O-deethylase (EROD), and cytosolic glutathione S-transferases (GSTs) activities were investigated using 7-ethoxyresorufin, 1-chloro-2,4-dinitrobenzene (CDNB), and ethacrynic acid (EA) as substrates, respectively. The average EROD activity was found as 1139±175 pmol resorufin/min/mg protein. The average GST activities towards CDNB and EA were found as 1364±41 and 140±19 nmol/min/mg protein, respectively. We have, then, investigated the in vitro effects of some metals and detergents on CYP1A and GST activities in leaping mullet liver. Leaping mullet liver microsomal EROD activity was significantly inhibited by Hg (0.1 mM), Ni (0.1 mM), Cd (0.1 mM), Cu (0.1 mM), Zn (0.1 mM), Sb (0.1 mM), Fe2+ (1 mM), Co (1 mM), Al (1 mM), and Fe3+ (1 mM), with the percent inhibition of 80, 80, 77, 75, 70, 69, 56, 53, 46, and 44, respectively. Similarly, conjugation of CDNB catalyzed by GST was inhibited significantly to lesser extend by Hg (0.1 mM), Sb (0.1 mM), Cd (0.1 mM), Cu (0.1 mM), Zn (0.1 mM), Fe3+ (1 mM), Co (1 mM), and Fe2+ (1 mM), with the percent inhibition of 70, 69, 65, 61, 54, 51, 47, and 43, respectively. The degrees of inhibition observed on GST catalyzed EA conjugation by Hg (0.1 mM), Cd (0.1 mM), Sb (0.1 mM), Cu (0.1 mM), and Zn (0.1 mM) were 86, 78, 69, 51, and 42, respectively. In addition to metals, the effect of various detergents on leaping mullet liver EROD, GST-CDNB, and GST-EA activities were studied. It was found that ionic detergents strongly inhibited the EROD activity, whereas much less inhibitions were observed with GST catalyzed activities. Therefore, the CYP1A inhibition potencies of metals and detergents suggest that their contribution to the overall CYP1A induction in polycyclic aromatic hydrocarbons contaminated environmental samples has to be taken into account for better interpretation of environmental studies. © 2006 Elsevier Inc. All rights reserved. | en_US |
dc.language.iso | en | en_US |
dc.relation.ispartof | Ecotoxicology and Environmental Safety | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | 7-Ethoxyresorufin O-deethylase | en_US |
dc.subject | Biomarkers | en_US |
dc.subject | Detergents | en_US |
dc.subject | Glutathione S-transferases | en_US |
dc.subject | Inhibition | en_US |
dc.subject | Liza saliens | en_US |
dc.subject | Metals | en_US |
dc.subject | Mullet | en_US |
dc.subject | 1 chloro 2,4 dinitrobenzene | en_US |
dc.subject | aluminum | en_US |
dc.subject | antimony | en_US |
dc.subject | cadmium | en_US |
dc.subject | cobalt | en_US |
dc.subject | copper | en_US |
dc.subject | cytochrome P450 1A | en_US |
dc.subject | detergent | en_US |
dc.subject | etacrynic acid | en_US |
dc.subject | ethoxyresorufin | en_US |
dc.subject | ethoxyresorufin deethylase | en_US |
dc.subject | ferrous ion | en_US |
dc.subject | glutathione | en_US |
dc.subject | glutathione transferase | en_US |
dc.subject | microsome enzyme | en_US |
dc.subject | nickel | en_US |
dc.subject | zinc | en_US |
dc.subject | biomarker | en_US |
dc.subject | biotransformation | en_US |
dc.subject | enzyme activity | en_US |
dc.subject | metal | en_US |
dc.subject | PAH | en_US |
dc.subject | perciform | en_US |
dc.subject | pollution effect | en_US |
dc.subject | aquatic environment | en_US |
dc.subject | aquatic species | en_US |
dc.subject | article | en_US |
dc.subject | conjugation | en_US |
dc.subject | controlled study | en_US |
dc.subject | detoxification | en_US |
dc.subject | enzyme inhibition | en_US |
dc.subject | enzyme substrate | en_US |
dc.subject | in vitro study | en_US |
dc.subject | liver | en_US |
dc.subject | liver microsome | en_US |
dc.subject | nonhuman | en_US |
dc.subject | statistical significance | en_US |
dc.subject | Animals | en_US |
dc.subject | Biological Markers | en_US |
dc.subject | Biotransformation | en_US |
dc.subject | Cytochrome P-450 CYP1A1 | en_US |
dc.subject | Dinitrochlorobenzene | en_US |
dc.subject | Environmental Monitoring | en_US |
dc.subject | Enzyme Inhibitors | en_US |
dc.subject | Ethacrynic Acid | en_US |
dc.subject | Fish Proteins | en_US |
dc.subject | Glutathione Transferase | en_US |
dc.subject | Liver | en_US |
dc.subject | Metabolic Detoxication, Drug | en_US |
dc.subject | Microsomes, Liver | en_US |
dc.subject | Oxazines | en_US |
dc.subject | Smegmamorpha | en_US |
dc.subject | Substrate Specificity | en_US |
dc.subject | Water Pollutants, Chemical | en_US |
dc.title | Effects of metals and detergents on biotransformation and detoxification enzymes of leaping mullet (Liza saliens) | en_US |
dc.type | Article | en_US |
dc.identifier.volume | 68 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.startpage | 405 | |
dc.identifier.startpage | 405 | en_US |
dc.identifier.endpage | 411 | en_US |
dc.identifier.doi | 10.1016/j.ecoenv.2006.08.007 | - |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.identifier.pmid | 17011620 | en_US |
dc.identifier.scopus | 2-s2.0-34848832885 | en_US |
dc.identifier.wos | WOS:000251067500011 | en_US |
dc.identifier.scopusquality | Q1 | - |
dc.owner | Pamukkale University | - |
item.grantfulltext | none | - |
item.openairetype | Article | - |
item.cerifentitytype | Publications | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
crisitem.author.dept | 17.02. Biology | - |
crisitem.author.dept | 20.03. Biomedical Engineering | - |
Appears in Collections: | Fen-Edebiyat Fakültesi Koleksiyonu PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection |
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