Rheological properties of heat-induced gels from egg albumin and bovine plasma proteins were measured using a mechanical loading device. Each protein was tested at 8per thousand protein concentration and heated for 0-20 min at 80°C in an agitating water bath. After heating, the viscosity index, apparent elasticity and initial penetration force of the gels were evaluated. Bovine plasma protein dispersions exhibited a substantially higher viscosity index, apparent elasticity and initial penetration force than egg albumin gels. Bovine plasma proteins produced a gel structure which was strong and elastic. By comparison, heat-induced gels of egg albumin proteins were fragile and somewhat brittle.