Data/hora: 02/06/2024 09:38:08

Provedor de dados: | Obihiro University of Agriculture and Veterinary Medicine Academic Repository (OAK)
País: | Japan
Título: | Characterization of a leucine aminopeptidase from Toxoplasma gondii
Autores: | Jia, Honglin; Nishikawa, Yoshifumi; Luo, Yuzi; Yamagishi, Junya; Sugimoto, Chihiro; Xuan, Xuenan.
Data: | 2010-03
Ano: | 2010
Palavras-chave: | Toxoplasma gondii; Leucine aminopeptidase; Enzymatic activity.
Resumo: | The M17 family leucine aminopeptidase (LAP) hydrolyze amino acids from the N-terminus of peptides. Many LAPs from parasitic protozoa including Plasmmodium, Trypanosoma and Leishmania, have been intensely investigated because of their crucial roles in parasite biology. In this study, a functional recombinant Toxoplasma gondii LAP (rTgLAP) was expressed in Escherichia coli and its enzymatic activity against synthetic substrates for aminopeptidase, as well as the cellular localization was determined. Our results indicated that TgLAP is a functional aminopeptidase in the cytoplasma of T. gondii.
Idioma: | Inglês
Identificador: | http://ir.obihiro.ac.jp/dspace/handle/10322/2822
Editor: | ELSEVIER
Formato: | application/pdf
Fonte: | Elsevier B.V.