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Biosci Biotechnol Biochem. 2014;78(4):574-81. doi: 10.1080/09168451.2014.885822. Epub 2014 May 9.

Purification and cDNA cloning of a lectin and a lectin-like protein from Apios americana Medikus tubers.

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a Laboratory of Food Molecular Functionality , College of Agriculture, Ibaraki University , Ibaraki , Japan.


An Apios americana lectin (AAL) and a lectin-like protein (AALP) were purified from tubers by chromatography on Butyl-Cellulofine, ovomucoid-Cellulofine, and DEAE-Cellulofine columns. AAL showed strong hemagglutinating activity toward chicken and goose erythrocytes, but AALP showed no such activity toward any of the erythrocytes tested. The hemagglutinating activity of AAL was not inhibited by mono- or disaccharides, but was inhibited by glycoproteins, such as asialofetuin and ovomucoid, suggesting that AAL is an oligosaccharide-specific lectin. The cDNAs of AAL and AALP consist of 1,093 and 1,104 nucleotides and encode proteins of 302 and 274 amino acid residues, respectively. Both amino acid sequences showed high similarity to known legume lectins, and those of their amino acids involved in carbohydrate and metal binding were conserved.


Apios americana; cDNA cloning; lectin; purification

[Indexed for MEDLINE]

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