Characterization of a lectin from the leaves of great northern bean, Phaseolus vulgaris L.
A novel lectin (GNLL) was isolated from the leaves of the Great Northern bean, Phaseolus vulgaris. GNLL was purified by affinity chromatography on ovomucoid-Sepharose 4B. GNLL had a molecular mass of 135 kDa on gel filtration and gave two bands on SDS-polyacrylamide gel electrophoresis (PAGE)(band A of 34.0 kDa and band B of 34.2 kDa). Binding assay of horseradish peroxidase (HRP)-glycoproteins to the bands electroblotted onto polyvinylidene difluoride (PVDF) membrane showed that both bands could bind to complex-type N-linked oligosaccharide chains in glycoproteins. The N-terminal amino acid sequences of both bands were identical through the 10 residues and identical to that of alpha-subunit of a pod lectin (pod-alpha-subunit) from the same bean. On the other hand, band B cross-reacted with monoclonal antibody against a seed lectin from the same bean, but band A did not.
Kamemura
K
K
Department of Agricultural Chemistry, Faculty of Bioresources, Mie University, Japan.
Ozeki
M
M
Furuichi
Y
Y
Umekawa
H
H
Takahashi
T
T
D000595:Amino Acid Sequence; D003429:Cross Reactions; D006735:Horseradish Peroxidase; D008969:Molecular Sequence Data; D010835:Phytohemagglutinins / Q000032:analysis*; D018515:Plant Leaves / Q000737:chemistry*; D037121:Plant Lectins; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid
D010835:Phytohemagglutinins; D037121:Plant Lectins; D006735:Horseradish Peroxidase