Chetty C S, Naidu R C, Rajendra W, Indira K, Swami K S
Arch Int Physiol Biochim. 1981 Feb;89(1):51-5. doi: 10.3109/13813458109069137.
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.
在六指蛙(Rana hexadactyla)的对侧和去神经支配的腓肠肌中,研究了AMP脱氨酶的底物(AMP)和辅因子(ATP)依赖性动力学参数。与对侧肌肉酶相比,去神经支配的肌肉酶的表观亲和力(Km)和最大速度(V)有所增加。发现去神经支配后活化能(ΔE)值降低,表明去神经支配的肌肉酶催化效率提高。