Autor: |
Storch S; Children's Hospital-Biochemistry, University of Hamburg, Germany., Kübler B, Höning S, Ackmann M, Zapf J, Blum W, Braulke T |
Jazyk: |
angličtina |
Zdroj: |
FEBS letters [FEBS Lett] 2001 Dec 14; Vol. 509 (3), pp. 395-8. |
DOI: |
10.1016/s0014-5793(01)03204-5 |
Abstrakt: |
In the circulation, most of the insulin-like growth factors (IGFs) are bound to a ternary 150 kDa complex with IGF-binding protein (IGFBP)-3 and the acid labile subunit. In the current study, we identify transferrin (Tf) by mass spectrometry, and immunoprecipitation as a component of a major IGF-binding fraction separated from human plasma. IGF ligand blotting, cross-linkage experiments and surface plasmon resonance spectrometry have been used to demonstrate the capability of Tf to bind IGFs specifically. In combination with Tf, IGFBP-3 showed a 5-fold higher affinity for IGF-II than IGFBP-3 alone. The data suggest that Tf may play an important role in regulating IGF/IGFBP-3 functions. |
Databáze: |
MEDLINE |
Externí odkaz: |
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