Abstract
Numerous procedures for improving the entry of aggregates and of large myosin subunits into disc gels were investigated. Both rabbit and bovine myosin behaved essentially the same during electrophoresis in urea. Aggregates of myosin and large and small subunits were found to enter and migrate in a 2·5% acrylamide gel in 7 m urea on using a continuous buffer system. Washing with low ionic strength buffer ( 0·04 m KCl prior to the addition of urea increased the proportion of migrating myosin. Storage of myosin aggregates in urea for periods up to three weeks increased the yield of electrophoretically migrating protein. The possible significance of these findings with regard to the properties of meat is discussed.
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