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The substrate (AMP) and co-factor (ATP)-dependent kinetic parameters of AMP-deaminase have been studied in the contralateral and denervated gastrocnemius muscles of frog, Rana hexadactyla. An increasing in apparent affinity (Km) and maximal velocity (V) were found with denervated muscle enzyme as compared to the contralateral muscle enzyme. The activation energy (delta E) values were found to be decreased on denervation suggesting increased catalytic efficiency of denervated muscle enzyme.
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