Reacquisition of quaternary structure by fully reduced and denatured seminal ribonuclease.
Air-regenerated monomers of bovine seminal ribonuclease have been found capable of reassociating into native dimers, whereas monomers refolded in the presence of a glutathione redox mixture do not reassociate into dimers [Smith, K. G., D'Alessio, G. and Schaffer, S. W. (1978) Biochemistry 17, 2633-2638]. 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 two sulfhydryls at sequence positions 31 and 32 of the seminal RNAase chain, forming in the native dimer the intersubunit disulfides, have been found to have an important role in the refolding of the monomeric intermediates, as well as in the regeneration of dimers.
D000388:Air; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003553:Cystine / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008297:Male; D008956:Models, Chemical; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D012260:Ribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D012661:Semen / Q000201:enzymology
D004220:Disulfides; D046911:Macromolecular Substances; D003553:Cystine; D012260:Ribonucleases