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

Vanhoof, G.; Goossens, F.; Juliano, M. A.; Juliano, L.; Hendriks, D.; Schatteman, K.; Lin, A. H.; Scharpe, S.

Artigo

Fecha

1997-01-01

Registro en:

Cytogenetics and Cell Genetics. Basel: Karger, v. 78, n. 3-4, p. 275-280, 1997.

0301-0171

http://repositorio.unifesp.br/handle/11600/25678

10.1159/000134671

WOS:000071902100026

http://repositorioslatinoamericanos.uchile.cl/handle/2250/4025339

Autor

Vanhoof, G.

Goossens, F.

Juliano, M. A.

Juliano, L.

Hendriks, D.

Schatteman, K.

Lin, A. H.

Scharpe, S.

Institución

Universidade Federal de São Paulo (Brasil)

Resumen

A 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.

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