Characterization of a Lectin from the Leaves of Great Northern Bean,Phaseolus vulgarisL.

摘要

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#x2013;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-typeN-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#x3b1;-subunit of a pod lectin (pod-#x3b1;-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.