Thermodynamic investigation of camel retina acetylcholinesterase inhibition by cyclophosphamide.

The present work addresses the estimation of energy parameters such as Gibb's free energy change (delta G), enthalpy change (delta H); entropy change (delta S) and activation energy (E a) of acetylcholinesterase (AChE, EC 3.1.1.7) from camel retina in the absence and presence of the antineoplastic drug cyclophosphamide (CP). A spectrophotometric method was used for the determination of AChE activity, which was the basis for determination of these parameters. The PZ factor (number of sterically and energetically favorable collisions occurring between CP and AChE) have also been studied in this investigation. The energy parameters obtained in the present investigation were compared with the values reported elsewhere.