Increased electrophoretic mobility of sodium sulfite-treated jack bean urease.

Sodium sulfite is a widely used activity-protective agent for the storage of urease. However, this reagent produces a 10% increase in the anodic electrophoretic mobility of native urease. Changes in the hydrodynamic properties of the enzyme are not involved in that modification. The observed change is related to an increased negative charge of the protein molecule in the presence of sodium sulfite. The results are discussed in terms of sulfitolysis of the single disulfide bond in the urease monomer. It is remarkable that the modification occurs at neutral pH. Our results show that removing sodium sulfite and reversing its effect by treatment with 2-mercaptoethanol are required prior to any study involving native urease.