Characterization of xenobiotic metabolizing enzymes in sturgeon (Acipenser baeri).
Identifieur interne : 000749 ( PubMed/Curation ); précédent : 000748; suivant : 000750Characterization of xenobiotic metabolizing enzymes in sturgeon (Acipenser baeri).
Auteurs : E F Perdu-Durand [France] ; J P CravediSource :
- Comparative biochemistry and physiology. B, Comparative biochemistry [ 0305-0491 ] ; 1989.
English descriptors
- KwdEn :
- 7-Alkoxycoumarin O-Dealkylase (metabolism), Animals, Benzo(a)pyrene (metabolism), Benzopyrene Hydroxylase (metabolism), Coumarins (metabolism), Dinitrochlorobenzene (metabolism), Epoxide Hydrolases (metabolism), Epoxy Compounds (metabolism), Fishes (metabolism), Gills (enzymology), Kidney (enzymology), Liver (enzymology), Microsomes, Liver (enzymology), NADPH-Ferrihemoprotein Reductase (metabolism), Nitrophenols (metabolism), Xenobiotics (metabolism).
- MESH :
- chemical , metabolism : 7-Alkoxycoumarin O-Dealkylase, Benzo(a)pyrene, Benzopyrene Hydroxylase, Coumarins, Dinitrochlorobenzene, Epoxide Hydrolases, Epoxy Compounds, NADPH-Ferrihemoprotein Reductase, Nitrophenols, Xenobiotics.
- enzymology : Gills, Kidney, Liver, Microsomes, Liver.
- metabolism : Fishes.
- Animals.
Abstract
1. Cytochrome P-450, NADPH-cytochrome c reductase, benzo(a)-pyrene hydroxylase (AHH), 7-ethoxycoumarin-O-deethylase (7-ECOD), epoxide hydrolase (EH), UDP-glucuronyltransferase (UDPGT) and glutathione S-transferase (GSHST) activities in sturgeon (Acipenser baeri) have been measured and partially characterized. 2. Cytochrome P-450-dependent monoxygenase (MO), EH, and conjugation reactions were detected in liver and to a lesser extent in kidney and gills. 3. Hepatic enzyme activities in the sturgeon were equally high or higher than in rainbow trout liver, with the exception of UDPGT whose activity was 14% of that in trout liver. 4. The MO and EH activities displayed the expected pH maxima of 7.5, whereas transferases were relatively independent of the pH in the 6.5-7.5 range. 5. The temperature optima for MO and EH were close to those reported in other fish species, whereas for conjugation reactions the temperature optima were 45 and 60 degrees C for GSHST and UDPGT respectively.
PubMed: 2509131
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B, Comparative biochemistry</title><idno type="ISSN">0305-0491</idno><imprint><date when="1989" type="published">1989</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>7-Alkoxycoumarin O-Dealkylase (metabolism)</term><term>Animals</term><term>Benzo(a)pyrene (metabolism)</term><term>Benzopyrene Hydroxylase (metabolism)</term><term>Coumarins (metabolism)</term><term>Dinitrochlorobenzene (metabolism)</term><term>Epoxide Hydrolases (metabolism)</term><term>Epoxy Compounds (metabolism)</term><term>Fishes (metabolism)</term><term>Gills (enzymology)</term><term>Kidney (enzymology)</term><term>Liver (enzymology)</term><term>Microsomes, Liver (enzymology)</term><term>NADPH-Ferrihemoprotein Reductase (metabolism)</term><term>Nitrophenols (metabolism)</term><term>Xenobiotics (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>7-Alkoxycoumarin O-Dealkylase</term><term>Benzo(a)pyrene</term><term>Benzopyrene Hydroxylase</term><term>Coumarins</term><term>Dinitrochlorobenzene</term><term>Epoxide Hydrolases</term><term>Epoxy Compounds</term><term>NADPH-Ferrihemoprotein Reductase</term><term>Nitrophenols</term><term>Xenobiotics</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Gills</term><term>Kidney</term><term>Liver</term><term>Microsomes, Liver</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">1. Cytochrome P-450, NADPH-cytochrome c reductase, benzo(a)-pyrene hydroxylase (AHH), 7-ethoxycoumarin-O-deethylase (7-ECOD), epoxide hydrolase (EH), UDP-glucuronyltransferase (UDPGT) and glutathione S-transferase (GSHST) activities in sturgeon (Acipenser baeri) have been measured and partially characterized. 2. Cytochrome P-450-dependent monoxygenase (MO), EH, and conjugation reactions were detected in liver and to a lesser extent in kidney and gills. 3. Hepatic enzyme activities in the sturgeon were equally high or higher than in rainbow trout liver, with the exception of UDPGT whose activity was 14% of that in trout liver. 4. The MO and EH activities displayed the expected pH maxima of 7.5, whereas transferases were relatively independent of the pH in the 6.5-7.5 range. 5. The temperature optima for MO and EH were close to those reported in other fish species, whereas for conjugation reactions the temperature optima were 45 and 60 degrees C for GSHST and UDPGT respectively.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2509131</PMID><DateCreated><Year>1989</Year><Month>12</Month><Day>21</Day></DateCreated><DateCompleted><Year>1989</Year><Month>12</Month><Day>21</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0305-0491</ISSN><JournalIssue CitedMedium="Print"><Volume>93</Volume><Issue>4</Issue><PubDate><Year>1989</Year></PubDate></JournalIssue><Title>Comparative biochemistry and physiology. B, Comparative biochemistry</Title><ISOAbbreviation>Comp. Biochem. Physiol., B</ISOAbbreviation></Journal><ArticleTitle>Characterization of xenobiotic metabolizing enzymes in sturgeon (Acipenser baeri).</ArticleTitle><Pagination><MedlinePgn>921-8</MedlinePgn></Pagination><Abstract><AbstractText>1. Cytochrome P-450, NADPH-cytochrome c reductase, benzo(a)-pyrene hydroxylase (AHH), 7-ethoxycoumarin-O-deethylase (7-ECOD), epoxide hydrolase (EH), UDP-glucuronyltransferase (UDPGT) and glutathione S-transferase (GSHST) activities in sturgeon (Acipenser baeri) have been measured and partially characterized. 2. Cytochrome P-450-dependent monoxygenase (MO), EH, and conjugation reactions were detected in liver and to a lesser extent in kidney and gills. 3. Hepatic enzyme activities in the sturgeon were equally high or higher than in rainbow trout liver, with the exception of UDPGT whose activity was 14% of that in trout liver. 4. The MO and EH activities displayed the expected pH maxima of 7.5, whereas transferases were relatively independent of the pH in the 6.5-7.5 range. 5. The temperature optima for MO and EH were close to those reported in other fish species, whereas for conjugation reactions the temperature optima were 45 and 60 degrees C for GSHST and UDPGT respectively.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Perdu-Durand</LastName><ForeName>E F</ForeName><Initials>EF</Initials><AffiliationInfo><Affiliation>I.N.R.A., Laboratoire des Xénobiotiques, Toulouse, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cravedi</LastName><ForeName>J P</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Comp Biochem Physiol B</MedlineTA><NlmUniqueID>2984730R</NlmUniqueID><ISSNLinking>0305-0491</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003374">Coumarins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004852">Epoxy Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009596">Nitrophenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015262">Xenobiotics</NameOfSubstance></Chemical><Chemical><RegistryNumber>31005-02-4</RegistryNumber><NameOfSubstance UI="C017299">7-ethoxycoumarin</NameOfSubstance></Chemical><Chemical><RegistryNumber>3417WMA06D</RegistryNumber><NameOfSubstance UI="D001564">Benzo(a)pyrene</NameOfSubstance></Chemical><Chemical><RegistryNumber>9QH06NGT6O</RegistryNumber><NameOfSubstance UI="C013690">styrene oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.13.-</RegistryNumber><NameOfSubstance UI="D015660">7-Alkoxycoumarin O-Dealkylase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.14.-</RegistryNumber><NameOfSubstance UI="D001579">Benzopyrene Hydroxylase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.2.4</RegistryNumber><NameOfSubstance UI="D009251">NADPH-Ferrihemoprotein Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.3.2.-</RegistryNumber><NameOfSubstance UI="D004851">Epoxide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GE3IBT7BMN</RegistryNumber><NameOfSubstance UI="D004137">Dinitrochlorobenzene</NameOfSubstance></Chemical><Chemical><RegistryNumber>Y92ZL45L4R</RegistryNumber><NameOfSubstance UI="C024836">4-nitrophenol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015660" MajorTopicYN="N">7-Alkoxycoumarin O-Dealkylase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001564" MajorTopicYN="N">Benzo(a)pyrene</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001579" MajorTopicYN="N">Benzopyrene Hydroxylase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003374" MajorTopicYN="N">Coumarins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004137" MajorTopicYN="N">Dinitrochlorobenzene</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004851" MajorTopicYN="N">Epoxide Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004852" MajorTopicYN="N">Epoxy Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005880" MajorTopicYN="N">Gills</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007668" MajorTopicYN="N">Kidney</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008862" MajorTopicYN="N">Microsomes, Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009251" MajorTopicYN="N">NADPH-Ferrihemoprotein Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009596" MajorTopicYN="N">Nitrophenols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015262" MajorTopicYN="N">Xenobiotics</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1989</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1989</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1989</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId 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