Conformational comparison of human pituitary growth hormone and human chorionic somatomammotropin (human placental lactogen) by second-order absorption spectroscopy.
Second-order absorption spectra strongly suggest the presence of a hydrogen bond between the single Trp of human pituitary growth hormone (hGH) and a carboxylate ion. This hydrogen-bonded complex is buried within the hydrophobic interior of the hGH molecule. Although the homologous Trp in human chorionic somatomammotropin [human placental lactogen, HCS(hPL)] is also buried within the hydrophobic interior of the molecule, there is no evidence that it is hydrogen bonded in the native protein. However, during the early stages of thermolysin digestion of HCS(hPL), both difference and second-order absorption spectra do indicate the transient presence of a similar hydrogen-bonded Trp-carboxylate complex. The molar extinction coefficients of hGH and HCS(hPL) have been refined.
D013006:Growth Hormone; D006801:Humans; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D010446:Peptide Fragments / Q000032:analysis; D010928:Placental Lactogen; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013820:Thermolysin
D010446:Peptide Fragments; D013006:Growth Hormone; D010928:Placental Lactogen; D013820:Thermolysin