The insulin-like growth factor (IGF) binding site of bovine insulin-like growth factor binding protein-2 (bIGFBP-2) probed by iodination.

The Journal of Biological Chemistry
G D HobbaJ C Wallace

Abstract

The insulin-like growth factor (IGF) binding site of bovine insulin-like growth factor binding protein 2 (bIGFBP-2) has been probed by chemical iodination. Tyrosyl residues of bIGFBP-2 were reacted by chloramine T-mediated iodination. The modification patterns of free bIGFBP-2 and bIGFBP-2 associated with insulin-like growth factor II (IGF-II) were compared by tryptic mapping using electrospray mass spectrometry and N-terminal sequencing. The presence of bound IGF-II resulted in protection of tyrosine at position 60 from iodination measured by the relative loss of tyrosine specific fluorescence and the incorporation of the radioisotope 125I. In addition, the pattern of iodine incorporation of bIGFBP-2 was not different whether IGF-I or IGF-II was the protective ligand. bIGFBP-2, when iodinated alone sustained a 8-fold loss of binding affinity for IGF-I and a 4-fold loss in binding affinity for IGF-II. In contrast, bIGFBP-2 iodinated while complexed with either IGF-I or IGF-II retained the same binding affinity for IGF-I or IGF-II as non-iodinated bIGFBP-2. We conclude that tyrosine 60 lies either in a region of bIGFBP-2 which directly interacts with both IGF-I and IGF-II or lies in a region of bIGFBP-2 which undergoes a conform...Continue Reading

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Citations

Dec 30, 2014·Cytokine & Growth Factor Reviews·V C RussoG A Werther
Apr 14, 2015·BioMed Research International·Varsha P BrahmkhatriHanudatta S Atreya
Aug 29, 1998·The Journal of Biological Chemistry·X QinS Mohan
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Dec 12, 2019·Frontiers in Endocrinology·Shumsuzzaman Khan

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