Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1214602 | Journal of Chromatography B | 2009 | 4 Pages |
Abstract
Association of IGFBP-1, IGFBP-2 and IGFBP-3 with other proteins in human serum and placental cell membranes was investigated using affinity chromatography matrix with immobilized antibodies. Circulating IGFBP-1 was found to be predominantly bound to α2-macroglobulin and not in the binary complex with its ligand, IGFBP-2 complexes and/or polymers were detected, which was not acknowledged before, and IGFBP-3 molecular forms were differentiated into those that form binary/ternary complexes and those that form stable associations with other serum proteins. As for placental membranes, both IGFBP-1 dimers and high molecular mass IGFBP-1 associations, most probably with α2-macroglobulin, were recognized and resolved.
Related Topics
Physical Sciences and Engineering
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Authors
Olgica Nedić, Romana Masnikosa,