Diversity of human insulin-like growth factor (IGF) binding protein-2 fragments in plasma: primary structure, IGF-binding properties, and disulfide bonding pattern.

@article{Mark2005DiversityOH,
  title={Diversity of human insulin-like growth factor (IGF) binding protein-2 fragments in plasma: primary structure, IGF-binding properties, and disulfide bonding pattern.},
  author={Silke Mark and Bernd K{\"u}bler and Stefan H{\"o}ning and Sandra Oesterreicher and Harald John and Thomas Braulke and W G Forssmann and Ludger Staendker},
  journal={Biochemistry},
  year={2005},
  volume={44 9},
  pages={3644-52}
}
The insulin-like growth factor binding proteins (IGFBPs) play a major role in the regulation of the effects and the bioavailability of the insulin-like growth factors (IGFs). IGFs are released from IGFBP-IGF complexes by proteolysis of IGFBPs generating fragments with reduced ligand-binding properties. To identify naturally occurring fragments of IGFBP-2, a peptide library generated from human hemofiltrate was immunologically screened. Purification of immunoreactive IGFBP-2 fragments was… CONTINUE READING
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