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Lectins from bulbs of the
Chinese daffodil Narcissus tazetta (family
Amaryllidaceae).
Ooi
LS, Ng
TB, Geng
Y, Ooi
VE.
Department of Biochemistry, The Chinese University of
Hong Kong, Shatin, NT.
The isolation of three lectins with
similar N-terminal amino acid sequences from the bulbs of the Chinese
daffodil Narcissus tazetta was achieved. The isolation protocol involved
ion exchange chromatography on DEAE-cellulose, affinity chromatography
on mannose-agarose, and fast protein liquid chromatography-gel
filtration on Superose 12. The lectins were all adsorbed on
mannose-agarose and demonstrated a single band with a molecular weight
of 13 kDa in SDS-polyacrylamide gel electrophoresis and a single 26 kDa
peak in gel filtration, indicating that they were mannose-binding,
dimeric proteins. The lectins differed in hemagglutinating activity,
with the magnitude of the activity correlating with the ionic strength
of the buffer required to elute the lectin from the DEAE-cellulose
column. The bulb lectin did not exert potent cytotoxicity against cancer
cell lines or fetal bovine lung cells but inhibited syncytium formation
in, and reinstated viability of, fetal bovine lung cells infected with
bovine immunodeficiency virus.
PMID: 11012085 [PubMed - indexed
for MEDLINE]
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