@Article{biocell.2005.29.187,
AUTHOR = {ZHONGHAI CHEN, YONGZHEN PANG, XIAOJUN LIU, XINGLONG WANG, ZHONGXIANG DENG, XIAOFEN SUN, KEXUAN TANG},
TITLE = {Molecular cloning and characterization of a novel mannosebinding lectin cDNA from <i>Zantedeschia aethiopica</i>},
JOURNAL = {BIOCELL},
VOLUME = {29},
YEAR = {2005},
NUMBER = {2},
PAGES = {187--193},
URL = {http://www.techscience.com/biocell/v29n2/37668},
ISSN = {1667-5746},
ABSTRACT = {Using RNA extracted from <i>Zantedeschia aethiopica</i> young leaves and primers designed according to the conservative regions of <i>Araceae</i> lectins, the full-length cDNA of <i>Z. aethiopica</i> agglutinin (ZAA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of <i>zaa</i> was 871 bp and contained a 417 bp open reading frame (ORF) encoding a lectin precursor of 138 amino acids. Through comparative analysis of <i>zaa</i> 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 <i>zaa</i> belonged to a multi-copy gene family.},
DOI = {10.32604/biocell.2005.29.187}
}