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1) Denaturation of carp actomyosin during storage at -20 degrees was studied with particular interest in the cryoprotective effect of sodium glutamate, the most cryoprotective of the compounds tested previously. 2) Storage with glutamate prevented the rapid decrease in solubility, viscosity, and ATPase (EC 3.6.1.3)activity of actomyosin during storage. Ultracentrifugal studies suggested that aggregation occurred in the frozen state without glutamate, but that added glutamate prevented aggregation or denaturation. 3) Electron microscopy showed that the original actomyosin consisted of long filaments with typical "arrowhead" structures, and that these decomposed into small fragments and sticked with globular portions, forming loosely packed aggregates during storage without glutamate. On storage with glutamate, the filaments were well preserved, and their fine structure was clearer than that of the original sample. 4) Preparations of actomyosin extracted with 10 mM glutamate were of better quality and their ultrastructure and physicochemical and biochemical properties showed increased stability on freezing. 5) Freeze-denaturation seems to involve complicated aggregation with transconformation of proteins besides the side-to-side aggregation discussed previously.