Abstract
Myosin monomer can be separated from aggregated myosin and heterogeneous low molecular weight contaminants by chromatography on 4% or 2% agarose. The monomer was characterized by its ATPase activity, which was constant across the peak, and its molecular weight (about 465,000). Chromatographic studies of aged samples show that aggregation is accompanied by the release of low molecular weight material. Molecular sieve chromatography provides a new approach to the purification of myosin which should be useful in studies on its molecular structure.
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