Reacquisition of quaternary structure by fully reduced and denatured seminal ribonuclease

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Abstract
Air-regenerated monomers of bovine seminal RNase were found capable of reassociating into native dimers, whereas monomers refolded in the presence of a glutathione redox mixture do not reassociate into dimers. The crucial step in the process of regeneration of dimers is an isomerization step, which the newly refolded monomers undergo in order to reassociate into dimers. The 2 SH at sequence positions 31 and 32 of the seminal RNase chain, forming in the native dimer the intersubunit disulfides, were found to have an important role in the refolding of the monomeric intermediates, as well as in the regeneration of dimers.