PARTICLE-SIZE AND SHAPE OF THERMALLY DENATURED BOVINE SERUM-ALBUMIN BY LIGHT-SCATTERING

Solutions of bovine serum albumin in various stages of thermal denaturation, ranging from very early to fairly advanced, were prepared in a light scattering cell. The molecular weights and the molecular sizes of the subsequent aggregate particles were determined by the light scattering method. In the early stages of thermal denaturation, in the presence of sodium chloride, the aggregate particles were fairly stable, growing essentially in rods, relatively uniform in size. In the absence of sodium chloride, the aggregate particles extended fairly widely and were not uniform in size even in the early stages. © 1979.