PortalPublikationenTransferrin binds insulin-like growth factors and affects bi...

Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3.

Standard

Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3. / Storch, Stephan; Kübler, B; Höning, S; Ackmann, M; Zapf, J; Blum, W; Braulke, T.

in: FEBS LETT, Jahrgang 509, Nr. 3, 3, 2001, S. 395-398.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Storch, S, Kübler, B, Höning, S, Ackmann, M, Zapf, J, Blum, W & Braulke, T 2001, 'Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3.', FEBS LETT, Jg. 509, Nr. 3, 3, S. 395-398. <http://www.ncbi.nlm.nih.gov/pubmed/11749962?dopt=Citation>

APA

Storch, S., Kübler, B., Höning, S., Ackmann, M., Zapf, J., Blum, W., & Braulke, T. (2001). Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3. FEBS LETT, 509(3), 395-398. [3]. http://www.ncbi.nlm.nih.gov/pubmed/11749962?dopt=Citation

Vancouver

Storch S, Kübler B, Höning S, Ackmann M, Zapf J, Blum W et al. Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3. FEBS LETT. 2001;509(3):395-398. 3.

Bibtex

@article{d66986e9276347199e7f0576afae45e1,
title = "Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3.",
abstract = "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.",
author = "Stephan Storch and B K{\"u}bler and S H{\"o}ning and M Ackmann and J Zapf and W Blum and T Braulke",
year = "2001",
language = "Deutsch",
volume = "509",
pages = "395--398",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3.

AU - Storch, Stephan

AU - Kübler, B

AU - Höning, S

AU - Ackmann, M

AU - Zapf, J

AU - Blum, W

AU - Braulke, T

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

M3 - SCORING: Zeitschriftenaufsatz

VL - 509

SP - 395

EP - 398

JO - FEBS LETT

JF - FEBS LETT

SN - 0014-5793

IS - 3

M1 - 3

ER -