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Abstract
When studying proteins, usually great effort is expended in insuring that the protein studied is highly purified. For example, crystallization or gel filtration may be undertaken in an attempt to free the protein of interest from contamination by other protein systems. There are times, however, when the results of experiments on the molecular and catalytic properties of proteins, as well as their regulatory characteristics, can not be accounted for by assuming a homogeneous population of molecules of the protein under investigation. In kinetic studies, when heterogeneous reactions are encountered, the problem is often one of distinguishing heterogeneous subunits from heterogeneous aggregates.





