In the b-galactosidase lab, why was o-nitrophenol-b-d-galactosidase (onpg) used?

In the 1950s, christian anfinsen demonstrated the renaturation of the protein ribonuclease (rnase) in vitro. after reduction (to reduce the disulfide links) and the addition of urea (to denature the protein), the protein was in an unfolded state. after removing the urea and the reducing agent, the protein refolded, with greater than 90% activity. if the urea were removed after oxidation occurred, the protein had less than 5% activity. why would the protein not refold correctly if the urea were removed after the reducing agent was removed? (in other words, what would happen if the urea were removed after oxidation? )