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Glycobiology, 2000, Vol. 10, No. 12 1325-1331
© 2000 Oxford University Press

Description of a monomeric prototype galectin from the lizard Podarcis hispanica

Dolores Solís, María I.F. López-Lucendo, Sergio León, Javier Varela2 and Teresa Díaz-Mauriño1

Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Serrano 119, E-28006 Madrid, Spain, and 2Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velazquez 144, E-28006 Madrid, Spain

Galectins are a continuously expanding family of ß-galactoside-binding lectins present in a variety of evolutionarily divergent animal species. Here we report, for the first time, that expression of galectins extends to the reptilia lineage of lizards. Up to five lactose-binding proteins were isolated from the lizard Podarcis hispanica by affinity chromatography on asialofetuin-Sepharose. The main component, which is most abundantly expressed in skin, was purified from this tissue and further characterized. Under native conditions the protein behaved as a monomer with a molecular mass of 14,500 Da and an isoelectric point of 6.3. Based on sequence homology of the 58 N-terminal amino acid residues with galectins, and on its demonstrated galactoside-binding activity, this lectin we named LG-14 (from Lizard Galectin and 14 kDa) is classified as a new member of the galectin family. LG-14 falls into and strengthen the still thinly populated category of monomeric prototype galectins.

1 To whom correspondence should be addressed


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