Abstract
A radioimmunoassay for the 15-amino acid fragment comprising residues 32–46 of the 22,000-dalton human growth hormone has been devised. The radioimmunoassay detects from 1 to 150 fmol of the synthetic peptide. The 12-amino acid peptide hGH (35–46) shows parallel displacement, but the sensitivity decreased 50% due to the deletion of the three amino acids. Displacement activity is lost from the synthetic peptides hGH (38–46) and hGH (43–46), and intact hGH itself shows no displacement. Disrupting the large loop of hGH by subtilisin cleavage or by reduction and alkylation of the S-S bridges imparts displacement activity parallel to that of hGH (32–46), and hGH (1–139) has similar activity. A plausible interpretation for these results is that native hGH has a tertiary structure that masks or obscures the sequence 32–46, the sequence being unmasked by release of constraints imposed by an intact large loop.
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VanderLaan, W.P., Ling, N., VanderLaan, E.F. et al. Study of human growth hormone structure with a radioimmunoassay specific for the fifteen amino acid fragment comprising hGH (32–46). J Protein Chem 2, 341–346 (1983). https://doi.org/10.1007/BF01025599
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DOI: https://doi.org/10.1007/BF01025599