Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe).
Identifieur interne : 000362 ( PubMed/Corpus ); précédent : 000361; suivant : 000363Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe).
Auteurs : Joëlle Forget ; Sandrine Livet ; François LeboulengerSource :
- Comparative biochemistry and physiology. Toxicology & pharmacology : CBP [ 1532-0456 ] ; 2002.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Acetylcholinesterase.
- chemical , isolation & purification : Acetylcholinesterase.
- chemical , metabolism : Acetylcholinesterase.
- chemical , pharmacology : Cholinesterase Inhibitors.
- enzymology : Copepoda.
- Animals, Isoelectric Focusing, Isoelectric Point, Kinetics, Molecular Weight, Substrate Specificity.
Abstract
Oligohaline copepods such as Eurytemora affinis are widespread in estuaries of northwestern Europe. These minute crustaceans are highly sensitive to contamination and thus serve as useful bioindicators for the monitoring of pollutant effects. The use of decreased cholinesterase (ChE) activity as a sublethal biomarker of exposure to neurotoxic compounds supposes that ChE has been defined in copepods. This study reports the partial purification and characterization of ChE extracted from E. affinis. Analysis by non-denaturing PAGE and by isoelectric focusing indicated that the enzyme is probably a single dimeric form of 140 KDa, with a pI of 6.2. This enzyme is likely an acetylcholinesterase (AChE) since it hydrolyzes acetylthiocholine iodide at a higher rate than other substrates, such as butyrylthiocholine and propionylthiocholine, at pH 7.0 and 25 degrees C, and is inhibited by eserine but not by iso-OMPA. The enzyme exhibited high sensitivity to some of the various pollutants tested. The kinetic properties of this ChE were compared with those of other invertebrate ChEs.
PubMed: 12039688
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pubmed:12039688Le document en format XML
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These minute crustaceans are highly sensitive to contamination and thus serve as useful bioindicators for the monitoring of pollutant effects. The use of decreased cholinesterase (ChE) activity as a sublethal biomarker of exposure to neurotoxic compounds supposes that ChE has been defined in copepods. This study reports the partial purification and characterization of ChE extracted from E. affinis. Analysis by non-denaturing PAGE and by isoelectric focusing indicated that the enzyme is probably a single dimeric form of 140 KDa, with a pI of 6.2. This enzyme is likely an acetylcholinesterase (AChE) since it hydrolyzes acetylthiocholine iodide at a higher rate than other substrates, such as butyrylthiocholine and propionylthiocholine, at pH 7.0 and 25 degrees C, and is inhibited by eserine but not by iso-OMPA. The enzyme exhibited high sensitivity to some of the various pollutants tested. The kinetic properties of this ChE were compared with those of other invertebrate ChEs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12039688</PMID><DateCreated><Year>2002</Year><Month>5</Month><Day>31</Day></DateCreated><DateCompleted><Year>2003</Year><Month>01</Month><Day>27</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1532-0456</ISSN><JournalIssue CitedMedium="Print"><Volume>132</Volume><Issue>1</Issue><PubDate><Year>2002</Year><Month>May</Month></PubDate></JournalIssue><Title>Comparative biochemistry and physiology. Toxicology & pharmacology : CBP</Title><ISOAbbreviation>Comp. Biochem. Physiol. C Toxicol. Pharmacol.</ISOAbbreviation></Journal><ArticleTitle>Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe).</ArticleTitle><Pagination><MedlinePgn>85-92</MedlinePgn></Pagination><Abstract><AbstractText>Oligohaline copepods such as Eurytemora affinis are widespread in estuaries of northwestern Europe. These minute crustaceans are highly sensitive to contamination and thus serve as useful bioindicators for the monitoring of pollutant effects. The use of decreased cholinesterase (ChE) activity as a sublethal biomarker of exposure to neurotoxic compounds supposes that ChE has been defined in copepods. This study reports the partial purification and characterization of ChE extracted from E. affinis. Analysis by non-denaturing PAGE and by isoelectric focusing indicated that the enzyme is probably a single dimeric form of 140 KDa, with a pI of 6.2. This enzyme is likely an acetylcholinesterase (AChE) since it hydrolyzes acetylthiocholine iodide at a higher rate than other substrates, such as butyrylthiocholine and propionylthiocholine, at pH 7.0 and 25 degrees C, and is inhibited by eserine but not by iso-OMPA. The enzyme exhibited high sensitivity to some of the various pollutants tested. The kinetic properties of this ChE were compared with those of other invertebrate ChEs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Forget</LastName><ForeName>Joëlle</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Laboratoire d'Ecotoxicologie (LEMA), UPRES-EA3222, Faculté des Sciences et Techniques, Université du Havre, 25 rue Philippe Lebon, Le Havre, France. joelle.forget@univ-lehavre.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Livet</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Leboulenger</LastName><ForeName>François</ForeName><Initials>F</Initials></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Comp Biochem Physiol C Toxicol Pharmacol</MedlineTA><NlmUniqueID>100959500</NlmUniqueID><ISSNLinking>1532-0456</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002800">Cholinesterase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.7</RegistryNumber><NameOfSubstance UI="D000110">Acetylcholinesterase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000110" MajorTopicYN="N">Acetylcholinesterase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002800" MajorTopicYN="N">Cholinesterase Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D033342" MajorTopicYN="N">Copepoda</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007526" MajorTopicYN="N">Isoelectric Point</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>6</Month><Day>1</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>1</Month><Day>28</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>6</Month><Day>1</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12039688</ArticleId><ArticleId IdType="pii">S1532045602000509</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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