Abstract:
:A lectin with a novel N-terminal amino acid sequence was purified from the rhizomes of Aspidistra elatior Blume by ammonium sulphate precipitation, ion exchange chromatography on diethylaminoethyl-Sepharose and carboxymethyl-Sepharose and gel filtration chromatography on Sephacryl S-100. The A. elatior Blume lectin (AEL) is a heterotetramer with a molecular mass of 56 kDa and composed of two homodimers consisting of two different polypeptides of 13.5 kDa and 14.5 kDa held together by noncovalent interactions. Hapten inhibition assay indicated that hemagglutinating activity of AEL towards rabbit erythrocytes could be inhibited by D-mannose, mannan, thyroglobulin and ovomucoid. The lectin was stable up to 70 degrees C, and showed maximum activity in a narrow pH range of 7.0-8.0. Chemical modification and spectrum analysis indicated that tryptophan, arginine, cysteine and carboxyl group residues were essential for its hemagglutinating activity. However, they might not be present in the active center, except some carboxyl group residues. AEL also showed significant in vitro antiproliferative activity towards Bre-04 (66%), Lu-04 (60%) and HepG2 (56%) of human cancer cell lines.
journal_name
Acta Biochim Biophys Sin (Shanghai)journal_title
Acta biochimica et biophysica Sinicaauthors
Xu X,Wu C,Liu C,Luo Y,Li J,Zhao X,Damme EV,Bao Jdoi
10.1111/j.1745-7270.2007.00305.xsubject
Has Abstractpub_date
2007-07-01 00:00:00pages
507-19issue
7eissn
1672-9145issn
1745-7270journal_volume
39pub_type
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