Molecular cloning and characterization of a novel mannose-binding lectin cDNA from Zantedeschia aethiopica
Biocell
;
29(2): 187-193, ago. 2005. ilus
Article
in English
| LILACS
| ID: lil-429674
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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Index:
LILACS (Americas)
Main subject:
Plant Proteins
/
Mannose-Binding Lectin
Language:
English
Journal:
Biocell
Journal subject:
Clulas
Year:
2005
Type:
Article
Affiliation country:
China
Institution/Affiliation country:
Fudan University/CN
/
Shangai Jiaotong University/CN
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