Substitution of specific amino acids in insulin-like growth factor (IGF) binding protein 5 alters heparin binding and its change in affinity for IGF-I response to heparin.

@article{Arai1996SubstitutionOS,
  title={Substitution of specific amino acids in insulin-like growth factor (IGF) binding protein 5 alters heparin binding and its change in affinity for IGF-I response to heparin.},
  author={Tadashi Arai and Jane Badley Clarke and Antony Parker and Walker H. Busby and Taek Joeng Nam and David Robert Clemmons},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 11},
  pages={
          6099-106
        }
}
Heparin binding to insulin-like growth factor (IGF)-binding protein 5 (IGFBP-5) leads to a 17-fold decrease in its affinity for IGF-I, and a region that contains several basic amino acids (Arg201-Arg218) may be involved in this affinity shift. In the present study, mutagenesis was used to analyze the effect of substitutions for basic amino acids in the Arg201-Arg218 region of IGFBP-5 on heparin-binding and the heparin-induced affinity shift. Nine mutant forms were prepared. Their association… CONTINUE READING

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