The chromatography of the meromyosins on diethylaminoethylcellulose

Abstract

In a previous chromatographic study of rabbit L-myosin (Perry, 1960) the distribution of aden- osine-triphosphatase activity in the main eluted fraction of this protein did not appear to be compatible with enzymic homogeneity. Brahms (1959, 1960) has also reported the separation of components of different adenosine-triphosphatase activity from rabbit myosin. The relation of these findings to the subunit structure of myosin is far from clear but they suggested that re-investigation of the distribution of adenosine-triphosphatase activity between the light and heavy mero- myosins There is accumulating evidence of the heterogeneity of the meromyosins (Lowey & Holtzer, 1959; Fryar & Gibbs, 1960; Szent-Gyorgyi, Cohen & Philpott, 1960) and the solubility properties of heavy meromyosin com- pared to myosin and to light meromyosin make this protein particularly suitable for chromato- graphic studies with diethylaminoethylcellulose.