Isolation of complexes formed between insulin-like growth factor-binding protein-3 and transferrin from the human serum | Zendy

Goran Miljuš | Zendy; Miomir Petrovic | Zendy; Olgica Nedić | Zendy

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Isolation of complexes formed between insulin-like growth factor-binding protein-3 and transferrin from the human serum

Author(s) -

Goran Miljuš,

Miomir Petrovic,

Olgica Nedić

Publication year - 2011

Publication title -

journal of the serbian chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.227

H-Index - 45

eISSN - 1820-7421

pISSN - 0352-5139

DOI - 10.2298/jsc110831211m

Subject(s) - transferrin , immunoprecipitation , insulin like growth factor binding protein , chemistry , growth factor , biochemistry , metabolism , plasma protein binding , monomer , iron binding proteins , antibody , insulin like growth factor , biology , receptor , gene , organic chemistry , immunology , polymer

Insulin-like growth factors (IGFs) play an important role in the regulation of cell growth, differentiation and metabolism. The amount of free, biologically active IGFs is regulated by the IGF-binding proteins (IGFBPs). IGFBP-3 is the most abundant binding protein and it is known to interact with other circulating proteins, including transferrin (Tf). In order to elucidate the possible role of IGF/IGFBP-3 in the iron metabolism, it is necessary to isolate IGFBP-3/Tf complexes. Several affinity-based techniques were employed. Results have shown that only double immunoprecipitation method with anti-Tf and anti-IGFBP-3 antibodies selectively separated complexes from other molecular forms, such as monomers, oligomers or fragments of IGFBP-3 and Tf. Isolated complexes can now be used to investigate the relationship between IGF/IGFBP-3 and iron, both in structural and metabolic tеrms

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