Abstract
It has long been known that globular protein molecules in concentrated aqueous solution can be converted into a different form by heating or use of denaturing agents. Under certain conditions of pH and ionic strength, elastic gels are formed. This work describes kinetic measurements of viscosity and elasticity close to the gel point (sol-gel transition) in bovine serum albumin solutions. These studies and optical rotation measurements near the gel point lend support to the conclusions of earlier structural studies on this system, that the gel is fibrillar in nature.
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