Dependence of human somatotropin activity on interchain disulfide bridges.

The importance of the disulfide bridges for human somatotropin activity is investigated. The activity of somatotropin is tested by the tibia, radioimmuno-, and radioligand assays. The cleavage of disulfide bridges by sulfitolysis, reduction with dithiothreitol, or oxidation with performic acid does not completely abolish hormone activity. There is only one exception: in the radioligand assay, oxidized somatotropin is not able to displace native somatotropin from rat liver membranes. The diminution of hormone activity is independent of the charges of the groups introduced to the cysteine residues. The radioimmuno- and radioligand assays are more sensitive to conformational alterations in the somatotropin molecule than the biological test system.