Separation of the molecular forms of the insulin-like growth factor (IGF)-Binding proteins by affinity chromatography.
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 alpha(2)-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 alpha(2)-macroglobulin, were recognized and resolved.
Nedić
Olgica
O
INEP-Institute for the Application of Nuclear Energy, University of Belgrade, Banatska 31b, 11080 Belgrade, Serbia.
Masnikosa
Romana
R
D000328:Adult; D002846:Chromatography, Affinity / Q000379:methods*; D005260:Female; D006801:Humans; D018969:Insulin-Like Growth Factor Binding Proteins / Q000097:blood / Q000737:chemistry* / Q000302:isolation & purification*; D008297:Male; D008875:Middle Aged; D010920:Placenta / Q000737:chemistry; D011485:Protein Binding
D018969:Insulin-Like Growth Factor Binding Proteins