Molecular cloning and characterization of a novel mannose-binding lectin cDNA from Zantedeschia aethiopica.
Biocell
; Biocell;29(2): 187-93, 2005 Aug.
Article
em En
| BINACIS
| ID: bin-38396
Biblioteca responsável:
AR1.1
ABSTRACT
Using RNA extracted from Zantedeschia aethiopica young leaves and primers designed according to the conservative regions of Araceae lectins, the full-length cDNA of Z. aethiopica agglutinin (ZAA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of zaa was 871 bp and contained a 417 bp open reading frame (ORF) encoding a lectin precursor of 138 amino acids. Through comparative analysis of zaa gene and its deduced amino acid sequence with those of other Araceae species, it was found that zaa encoded a precursor lectin with signal peptide. Secondary and three-dimensional structure analyses showed that ZAA had many common characters of mannose-binding lectin superfamily and ZAA was a mannose-binding lectin with three mannose-binding sites. Southern blot analysis of the genomic DNA revealed that zaa belonged to a multi-copy gene family.
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Coleções:
06-national
/
AR
Base de dados:
BINACIS
Idioma:
En
Revista:
Biocell
Ano de publicação:
2005
Tipo de documento:
Article
País de publicação:
Argentina