Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)

dc.contributorUniv Instelling Antwerp
dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.creatorVanhoof, G.
dc.creatorGoossens, F.
dc.creatorJuliano, M. A.
dc.creatorJuliano, L.
dc.creatorHendriks, D.
dc.creatorSchatteman, K.
dc.creatorLin, A. H.
dc.creatorScharpe, S.
dc.date.accessioned2016-01-24T12:30:17Z
dc.date.accessioned2022-10-07T20:57:30Z
dc.date.available2016-01-24T12:30:17Z
dc.date.available2022-10-07T20:57:30Z
dc.date.created2016-01-24T12:30:17Z
dc.date.issued1997-01-01
dc.identifierCytogenetics and Cell Genetics. Basel: Karger, v. 78, n. 3-4, p. 275-280, 1997.
dc.identifier0301-0171
dc.identifierhttp://repositorio.unifesp.br/handle/11600/25678
dc.identifier10.1159/000134671
dc.identifierWOS:000071902100026
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/4025339
dc.description.abstractA novel human cDNA (XPNPEPL) encoding a protein of 623 amino acids exhibiting 44% sequence identity and 62% sequence similarity to pig kidney X-prolyl aminopeptidase (aminopeptidase P; EC 3.4.11.9) was obtained by reverse transcription/polymerase chain reaction of phytohemagglutinin-stimulated lymphocyte mRNA. Conserved sequences were found with the prokaryotic X-prolyl aminopeptidase encoding gene (pepP). the human gene translation product exhibits a high sequence homology to the Schizosaccharomyces pombe chromosome I hypothetical protein C22G7.01c and to the S. cerevisiae ORF y11029w. Northern blot analysis indicates an ubiquitous expression of the human XPNPEPL sequence.
dc.languageeng
dc.publisherKarger
dc.relationCytogenetics and Cell Genetics
dc.rightshttp://www.karger.com/Services/RightsPermissions
dc.rightsAcesso restrito
dc.titleIsolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)
dc.typeArtigo


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