Purification of Galectin-3 from Ovine Placenta: Developmentally Regulated Expression and immunological relevance

IIGLESIAS MM; RABINOVICH GA; AMBROSIO A; CASTAGNA L; SOTOMAYOR CE; WOLFENSTEIN-TODEL C

OXFORD UNIV PRESS INC

Lugar: Oxford; Año: 1998 vol. 8 p. 59 - 59

alectins, β-galactoside-binding lectins, are extensively distributed in the animal kingdom and share some basic molecular properties. Galectin-3, a member of this family, is generally associated with differentiation, morphogenesis, and metastasis. In this study, galectin-3 was isolated from ovine placental cotyledons round the middle of the gestation period by lactose extraction followed by affinity chromatography on lactosyl-agarose, and separated from galectin-1 by size exclusion chromatography on a Superose 12 column. Under native conditions this lectin behaved as a monomer with an apparent molecular weight of ∼29,000 and an isoelectric point of 9.0. The partial amino acid sequence of the peptides obtained by tryptic digestion of this protein followed by HPLC separation showed striking homology with other members of the galectin-3 subfamily. Furthermore, ovine placental galectin-3 exhibited specific mitogenic activity toward rat spleen mononuclear cells.