Characterization of a Lectin from the Leaves of Great Northern Bean, Phaseolus vulgaris L
A novel lectin (GN L L) was isolated from the leaves of the Great Northern bean, Phaseolus vulgaris. GN L L was purified by affinity chromatography on ovomucoid-Sepharose 4B. GN L L had a molecular mass of 135 kDa on gel filtration and gave two bands on SDS-polyacrylamide gel electrophoresis (PAGE)...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 60; no. 4; pp. 608 - 611 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
Taylor & Francis
1996
Japan Society for Bioscience Biotechnology and Agrochemistry Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | A novel lectin (GN
L
L) was isolated from the leaves of the Great Northern bean, Phaseolus vulgaris. GN
L
L was purified by affinity chromatography on ovomucoid-Sepharose 4B. GN
L
L 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 α-subunit of a pod lectin (pod-α-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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.60.608 |