In binding tests using Des-(1-3)-IGF-I and another analog, specific B-domain residues appeared critical for binding all tested IGFBPs.
In plain wordsIn lab tests with Des-(1-3)-IGF-I and another analog, B-domain residues appeared important for binding IGF binding proteins.
- Peptide
- IGF-1 DES (des(1-3)IGF-I)
- Outcome
- Not applicableB-domain contributions to IGFBP binding
- Study
n: not reported in source
Purified IGF binding proteins- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
Studies with [Gln3,Ala4,Tyr15,Leu16]IGF-I and Des-(1-3)-IGF-I indicate that specific residues in the first 16 amino acids of the B domain of IGF-I appear to be critical for binding to all of the IGFBPs tested, but not to IGF receptors.
2 context sentences(design, population, supporting numbers)
We have characterized the affinities of IGFBP-1-4 for IGF-I and -II by employing 1) purified IGFBP preparations, 2) both [125I]IGF-I and [125I]IGF-II as radioligands, and 3) multiple IGF analogs designed to have altered affinities for IGFBPs.
To this end, human (h) IGFBP-1, hIGFBP-2, and rat (r) IGFBP-4 have been purified to homogeneity from human amniotic fluid, human prostate epithelial cell culture, and B104 rat neuroblastoma cells; for human IGFBP-3, the glycosylated recombinant form (rec-hIGFBP-3), produced in Chinese hamster ovary cells, was employed.
In this study, IGF-1 DES (des(1-3)IGF-I) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking IGF-1 DES (des(1-3)IGF-I).