Isolation and characterisation of metallothionein from the clam Ruditapes decussatus

Detalhes bibliográficos
Autor(a) principal: Simes, D
Data de Publicação: 2003
Outros Autores: Bebianno, Maria João, Moura, José J. G.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.1/11748
Resumo: Metallothioneins (MT) were obtained after purification from metal-exposed clams (Ruditapes decussatus) using gel-permeation and ion-exchange chromatography. Four cadmium-metallothioneins (CdMTs) were resolved by ion-exchange chromatography and they all had similar molecular weights, high cadmium content and an absorption spectra indicative of the presence of characteristic Cd-S aggregates. The NH2-terminal sequence suggests the presence of at least two class I clam MT isoforms. For the other two putative clam CdMTs isolated, the results of the amino acid determination were inconclusive. One was slightly contaminated and the other one had a blocked NH2-terminal. These clam metalothioneins contain glycine, which seems to be a common feature of molluscan MT family and exhibited more similarity to oysters than to mussels. Further investigation on the inducibility of these isoforms will be necessary if clams are to be used as biomarkers of metal exposure.
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spelling Isolation and characterisation of metallothionein from the clam Ruditapes decussatusMolluscan metallothioneinsMass spectrometryCrystal structurePurificationCadmiumAcidSequencesProteinsBindingCdnaMetallothioneinClamRuditapes decussatusCdToxicityMetallothioneins (MT) were obtained after purification from metal-exposed clams (Ruditapes decussatus) using gel-permeation and ion-exchange chromatography. Four cadmium-metallothioneins (CdMTs) were resolved by ion-exchange chromatography and they all had similar molecular weights, high cadmium content and an absorption spectra indicative of the presence of characteristic Cd-S aggregates. The NH2-terminal sequence suggests the presence of at least two class I clam MT isoforms. For the other two putative clam CdMTs isolated, the results of the amino acid determination were inconclusive. One was slightly contaminated and the other one had a blocked NH2-terminal. These clam metalothioneins contain glycine, which seems to be a common feature of molluscan MT family and exhibited more similarity to oysters than to mussels. Further investigation on the inducibility of these isoforms will be necessary if clams are to be used as biomarkers of metal exposure.ElsevierSapientiaSimes, DBebianno, Maria JoãoMoura, José J. G.2018-12-07T14:57:53Z2003-052003-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11748eng0166-445X10.1016/S0166-445X(02)00185-6info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-11-29T10:41:49Zoai:sapientia.ualg.pt:10400.1/11748Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-11-29T10:41:49Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
title Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
spellingShingle Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
Simes, D
Molluscan metallothioneins
Mass spectrometry
Crystal structure
Purification
Cadmium
Acid
Sequences
Proteins
Binding
Cdna
Metallothionein
Clam
Ruditapes decussatus
Cd
Toxicity
title_short Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
title_full Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
title_fullStr Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
title_full_unstemmed Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
title_sort Isolation and characterisation of metallothionein from the clam Ruditapes decussatus
author Simes, D
author_facet Simes, D
Bebianno, Maria João
Moura, José J. G.
author_role author
author2 Bebianno, Maria João
Moura, José J. G.
author2_role author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv Simes, D
Bebianno, Maria João
Moura, José J. G.
dc.subject.por.fl_str_mv Molluscan metallothioneins
Mass spectrometry
Crystal structure
Purification
Cadmium
Acid
Sequences
Proteins
Binding
Cdna
Metallothionein
Clam
Ruditapes decussatus
Cd
Toxicity
topic Molluscan metallothioneins
Mass spectrometry
Crystal structure
Purification
Cadmium
Acid
Sequences
Proteins
Binding
Cdna
Metallothionein
Clam
Ruditapes decussatus
Cd
Toxicity
description Metallothioneins (MT) were obtained after purification from metal-exposed clams (Ruditapes decussatus) using gel-permeation and ion-exchange chromatography. Four cadmium-metallothioneins (CdMTs) were resolved by ion-exchange chromatography and they all had similar molecular weights, high cadmium content and an absorption spectra indicative of the presence of characteristic Cd-S aggregates. The NH2-terminal sequence suggests the presence of at least two class I clam MT isoforms. For the other two putative clam CdMTs isolated, the results of the amino acid determination were inconclusive. One was slightly contaminated and the other one had a blocked NH2-terminal. These clam metalothioneins contain glycine, which seems to be a common feature of molluscan MT family and exhibited more similarity to oysters than to mussels. Further investigation on the inducibility of these isoforms will be necessary if clams are to be used as biomarkers of metal exposure.
publishDate 2003
dc.date.none.fl_str_mv 2003-05
2003-05-01T00:00:00Z
2018-12-07T14:57:53Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.1/11748
url http://hdl.handle.net/10400.1/11748
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0166-445X
10.1016/S0166-445X(02)00185-6
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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