Abstract
The particle weight of crystalline egg albumin was detd. by the light-scattering method. Aggregation phenomena were observed as pH 4.2, i.e., within the usually accepted pH range of stability. Whereas the turbidity increased linearly with time, the rate of this increase, coinciding with the progress of aggregation, was particularly dependent on the concn. and temp. of the solution. During the aggregation no increase in free sulfhydryl groups could be detected, and the protein did not seem to have its ability to crystallize impaired.
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