Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli
Autor(a) principal: | |
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Data de Publicação: | 1989 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/6141 |
Resumo: | DNA molecules coding either for mature porcine D-amino acid oxidase or for truncated forms of the enzyme have been obtained by stepwise addition of synthetic oligonucleotides to a partial cDNA. Under the control of the λ P(L) thermoregulatable promoter, these DNAs were respectively expressed in Escherichia coli as 36, 28 and 25 kilodalton polypeptides, specifically recognised by antibodies raised against the natural enzyme. None of the truncated proteins were biologically active whereas the mature recombinant species was able to hydrolyze D-alanine in vitro as efficiently as the natural product. |
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Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coliDNA molecules coding either for mature porcine D-amino acid oxidase or for truncated forms of the enzyme have been obtained by stepwise addition of synthetic oligonucleotides to a partial cDNA. Under the control of the λ P(L) thermoregulatable promoter, these DNAs were respectively expressed in Escherichia coli as 36, 28 and 25 kilodalton polypeptides, specifically recognised by antibodies raised against the natural enzyme. None of the truncated proteins were biologically active whereas the mature recombinant species was able to hydrolyze D-alanine in vitro as efficiently as the natural product.ElsevierSapientiaCiccarelli, E.Massaer, M.Guillaume, J. P.Herzog, A.Loriau, R.Cravador, A.Jacobs, P.Bollen, A.2015-06-15T09:15:52Z19891989-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/6141eng0006-291XAUT: ACR00659;info: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:RCAAP2023-07-24T10:17:24Zoai:sapientia.ualg.pt:10400.1/6141Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:59:00.868285Repositório 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 |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
title |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
spellingShingle |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli Ciccarelli, E. |
title_short |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
title_full |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
title_fullStr |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
title_full_unstemmed |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
title_sort |
Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli |
author |
Ciccarelli, E. |
author_facet |
Ciccarelli, E. Massaer, M. Guillaume, J. P. Herzog, A. Loriau, R. Cravador, A. Jacobs, P. Bollen, A. |
author_role |
author |
author2 |
Massaer, M. Guillaume, J. P. Herzog, A. Loriau, R. Cravador, A. Jacobs, P. Bollen, A. |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Ciccarelli, E. Massaer, M. Guillaume, J. P. Herzog, A. Loriau, R. Cravador, A. Jacobs, P. Bollen, A. |
description |
DNA molecules coding either for mature porcine D-amino acid oxidase or for truncated forms of the enzyme have been obtained by stepwise addition of synthetic oligonucleotides to a partial cDNA. Under the control of the λ P(L) thermoregulatable promoter, these DNAs were respectively expressed in Escherichia coli as 36, 28 and 25 kilodalton polypeptides, specifically recognised by antibodies raised against the natural enzyme. None of the truncated proteins were biologically active whereas the mature recombinant species was able to hydrolyze D-alanine in vitro as efficiently as the natural product. |
publishDate |
1989 |
dc.date.none.fl_str_mv |
1989 1989-01-01T00:00:00Z 2015-06-15T09:15:52Z |
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/10400.1/6141 |
url |
http://hdl.handle.net/10400.1/6141 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0006-291X AUT: ACR00659; |
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 |
|
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1799133210576158720 |