| Registro completo |
| Provedor de dados: |
OAK
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| País: |
Japan
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| Título: |
Characterization of a leucine aminopeptidase from Toxoplasma gondii
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| Autores: |
Jia, Honglin
Nishikawa, Yoshifumi
Luo, Yuzi
Yamagishi, Junya
Sugimoto, Chihiro
Xuan, Xuenan
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| Data: |
2010-03
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| Ano: |
2010
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| Palavras-chave: |
Toxoplasma gondii
Leucine aminopeptidase
Enzymatic activity
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| 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.
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| Idioma: |
Inglês
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| Identificador: |
http://ir.obihiro.ac.jp/dspace/handle/10322/2822
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| Editor: |
ELSEVIER
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| Formato: |
application/pdf
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| Direitos: |
Elsevier B.V.
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