Interaction Between Ovomucoid and Lysozyme

The interaction between ovomucoid and lysozyme was investigated by precipitation experiments, polyacrylamide gel electrophoresis and inactivation experiments on ovomucoid. The ovomucoid-lysozyme mixture produced turbidity at low salt concentrations over the pH range 6–11. Although both ovomucoid and lysozyme solutions (0.2%, pH 8.5) yielded no precipitation when heated separately at 80°C for 10 mm, about 40% of the proteins in the 0.2% solution of the ovomucoid-lysozyme mixture (2:3, in weight; 1:3, in mole) was precipitated by the same treatment. Ovomucoid was found to form complexes with lysozyme, some of which were precipitated by centrifugation (2000 ×g, 20 mm), and it was presumed that ovomucoid and lysozyme molecules were brought close together by the electrostatic attractive force, unfolded by heating, and then aggregated through intermolecular forces such as hydrophobic forces, hydrogen bonds and disulfide bonds.