Abstract
A kinetic analysis was made, in some details, of the published data showing the rates of denaturation of carp muscle actomyosin or myofibrils in the frozen KCI solution.
The logarithm of protein solubility or ATPase activity were correlated by two straight lines with different slopes in plotting against storage time. However, the first-order rate constants decreased significantly with the storage time. When the reciprocals of protein solubility or activity were plotted against storage time, a straight line was obtained throughout the almost entire storage period. The second-order rate constants were reasonably constant for the storage period. The reaction order of denaturation was approximately 3/2 to 5/2, as estimated by the differential method from the denaturation curves. The facts indicate that the reaction of freeze-denaturation in KCI solution is not of first-order, but of around second-order. The applicability of the first-order and second-order rate constants as a measure in evaluating the variables effect on denaturation was discussed.
