%0 Journal Article
%T Isolation and characterization of galectin-1 binding proteins from human placenta
%A MIROSLAVA JANKOVIC
%J Journal of the Serbian Chemical Society
%D 2000
%I Serbian Chemical Society
%X Galectin-1 binding proteins were isolated from human placenta by affinity chromatography on a column with immobilized endogenous lectin. The molecular masses of the isolated proteins of 170, 67 and 56 kDa were estimated by gel filtration and SDS-PAGE. These proteins were characterized as galactose-containing glycoproteins, based on their reactivity with Ricinus communis agglutinin. In addition, sialylated-lacto-N-fucopentaose II was detected in the 170 kDa protein, using anti CA 19-9 monoclonal antibodies. The interaction of the isolated proteins with human placental galectin-1 was investigated by a solid phase binding assay using asialofetuin as the glycoprotein ligand. The 67 kDa and 56 kDa proteins were found to inhibit galectin-1 binding of asialofetuin, whereas the 170 kDa protein had the opposite effect. It caused an increase in the binding of asialofetuin, suggesting a positive cooperative binding.
%K galectin-1
%K human placenta
%K affinity chromatography
%K RCA I
%K CA19-9
%U http://www.shd.org.yu/HtDocs/SHD/Vol65/No2-Pdf/V65-No2-07.zip