Isolation and characterization of galectin-1 binding proteins from human placenta
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...
| Main Author: | |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Serbian Chemical Society
2000-01-01
|
| Series: | Journal of the Serbian Chemical Society |
| Subjects: | |
| Online Access: | http://www.doiserbia.nb.rs/img/doi/0352-5139/2000/0352-51390002131J.pdf |
| Summary: | 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. |
|---|---|
| ISSN: | 0352-5139 1820-7421 |