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Porcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli

dc.contributor.authorCiccarelli, E.
dc.contributor.authorMassaer, M.
dc.contributor.authorGuillaume, J. P.
dc.contributor.authorHerzog, A.
dc.contributor.authorLoriau, R.
dc.contributor.authorCravador, A.
dc.contributor.authorJacobs, P.
dc.contributor.authorBollen, A.
dc.date.accessioned2015-06-15T09:15:52Z
dc.date.available2015-06-15T09:15:52Z
dc.date.issued1989
dc.description.abstractDNA 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.
dc.identifier.issn0006-291X
dc.identifier.otherAUT: ACR00659;
dc.identifier.urihttp://hdl.handle.net/10400.1/6141
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier
dc.relation.isbasedonP-008-R63
dc.titlePorcine D-amino acid oxidase: production of the biologically active enzyme in Escherichia coli
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage872
oaire.citation.startPage865
oaire.citation.titleBiochemical and Biophysical Research Communications
oaire.citation.volume161
person.familyNameCravador
person.givenNameAlfredo
person.identifier.orcid0000-0002-9831-9815
person.identifier.ridK-7247-2012
person.identifier.scopus-author-id6602537257
rcaap.rightsopenAccess
rcaap.typearticle
relation.isAuthorOfPublication8c84a9e6-6b7f-4b50-93a2-152c85901722
relation.isAuthorOfPublication.latestForDiscovery8c84a9e6-6b7f-4b50-93a2-152c85901722

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