Reaction of human choriomammotropin with hydrogen peroxide.

Treatment of human choriomammotropin with hydrogen peroxide in the absence of denaturant was found to oxidize five of its six methionine residues to sulfoxide; the residue not oxidized was found to be methionine-170. This derivative was identical to the native hormone by exclusion chromatography, circular dichroism spectra, and rate of tryptic digestion, but suffered a very substantial drop in biological activity. In the presence of 8 M urea all of the methionines could be oxidized with hydrogen peroxide or alkylated with iodoacetic acid. The physical properties of these completely methionine-modified derivatives were significantly changed and biological activity had again been very substantially decreased. In control experiments, treatment of the native hormone with 8 M urea did not affect its physical, spectral or biological properties. Amino acid analysis of the derivatives was completely in accord with that expected.