Abstract
Effect of pH (5.5-8.0) on filament-forming ability and biochemical activity of carp, tilapia, and rabbit myosins were studied. In the acidic pH range, both filament-forming ability and actin-activation of Mg-ATPase of the three myosins tended to increase. When the Mg-ATPase was strongly actin-activated and the activity was saturated by a small amount of actin, bipolar filaments whose thickness and length were more than 290A and more than 0.7μm, respectively, were formed. Tilapia myosin unusually formed the bipolar filaments only in acidic condition. Changes in light scattering intensity of each myosin suspension suggested that the bipolar filaments might be in a rigid form, because they hardly dissociated into small myosin filaments by treatment with KCl or ATP.
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