Myosin changes during frozen storage

Jarenback and Liljemark (75,76) found similar changes in cod actomyosin solution and cod muscle during frozen storage. The denatured myosin was not extracted with salt solution. 

Changes in solubility, viscosity, ATPase activity, and ultracentrifugal and salting-out profiles were found during frozen storage at -20°C of carp myosin solutions (in 0.6 M KC1) and carp myosin suspensions (in 0.05 M KC1) (82,93). 

Data on myosin (50,51,82,91) and LMM (82) support side-to-side aggregation of molecules without appreciable change in conformation during frozen storage, as proposed by Connell (91). 

Changes in the shape of carp actomyosin filaments during frozen storage was also studied at various pH s (67). Pictures of actomyosin frozen and stored in 0.9M and 1.2M KC1 illustrated the dissociation of actomyosin into actin and myosin (1,2). 

The susceptibility to conformational changes is also governed by the formation of FA in the fish muscle. Structural changes during frozen storage in cod myosin, for instance, were noted to be induced by the addition of FA (Careche and Li-Chan,... 

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