- Joined
- Nov 19, 2009
- Messages
- 257
IGF-I (1-3) represents the N-terminal tripeptide fragment GPE of the insulin-like growth factor 1 and, probably, its active site.
This N-terminal tripeptide of IGF-I facilitated the in vitro release of acetylcholine with a several hundredfold higher potency (10⁻¹⁰ - 10⁻⁶ M) than intact IGF-I (4 · 10⁻⁸ M), whereas truncated IGF-I lacking the tripeptide GPE, did not show any significant effect. This raises the possibility that GPE may be the active site of IGF-I.
Igf-1 des(1-3) is the missing part of the GPE with 67 peptide
conclusion igf-1 des(1-3) is less powerful than gpe igf-1(1-3)
This N-terminal tripeptide of IGF-I facilitated the in vitro release of acetylcholine with a several hundredfold higher potency (10⁻¹⁰ - 10⁻⁶ M) than intact IGF-I (4 · 10⁻⁸ M), whereas truncated IGF-I lacking the tripeptide GPE, did not show any significant effect. This raises the possibility that GPE may be the active site of IGF-I.
Igf-1 des(1-3) is the missing part of the GPE with 67 peptide
conclusion igf-1 des(1-3) is less powerful than gpe igf-1(1-3)
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