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Parasitol Int ; 49(4): 301-7, 2000 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-11077264

RESUMO

We have previously identified and characterized two amastigote-specific cysteine proteinases of Leishmania pifanoi. The slightly different isoforms of the more abundant proteinase are coded by a gene family of approximately 20 gene copies, that contain a C-terminal extension characteristic of cysteine proteinases of trypanosomatids. In this gene family, we have detected a copy that codes for a truncated form of this proteinase, lacking the C-terminal extension. Interestingly, when the deletion of a nucleotide that creates a stop codon causing this truncation is disregarded, the translated sequence gives rise to a divergent C-terminal extension that has many conserved amino acids when compared to Leishmania and Trypanosome, suggesting that a recent mutation led to the truncation.


Assuntos
Cisteína Endopeptidases/genética , Leishmania/enzimologia , Mutação , Sequência de Aminoácidos , Animais , Sequência de Bases , Mapeamento Cromossômico , Cisteína Endopeptidases/química , Cisteína Endopeptidases/metabolismo , Dosagem de Genes , Leishmania/genética , Dados de Sequência Molecular , Análise de Sequência de DNA
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