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 inBioscience, biotechnology, and biochemistry Vol. 60; no. 4; pp. 608 - 611
Main Authors Kamemura, Kazuo, Ozeki, Munetaka, Furuichi, Yukio, Umekawa, Hayato, Takahashi, Takao
Format Journal Article
LanguageEnglish
Published Tokyo Taylor & Francis 1996
Japan Society for Bioscience Biotechnology and Agrochemistry
Oxford University Press
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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.
Bibliography:ObjectType-Article-1
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ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.60.608