ABSTRACT
Acetylcholinesterase (ACE) activity and lipid peroxidation (LPO) parameters were measured in the blood of patients with Alzheimer's disease (AD) during treatment with amiridine and gliatiline. Treatment was accompanied by inhibition of ACE. There was a statistically significant relationship between clinical efficacy and changes in ACE activity. AD was charactefized by significant changes in LPO parameters, with a three-fold increase in the level of primary oxidation products on the background of a sharp (seven-fold) increase in total lipid desaturatedness. There was a statistically significant relationship between ACE activity and the levels of primary oxidation products in the RBC of patients with AD before and after treatment with amiridine and gliatiline.
Subject(s)
Alzheimer Disease/blood , Alzheimer Disease/drug therapy , Aminoquinolines , Cholinergic Agents/therapeutic use , Acetylcholinesterase/blood , Aged , Butyrylcholinesterase/blood , Cholinesterase Inhibitors/therapeutic use , Erythrocytes/drug effects , Erythrocytes/enzymology , Female , Humans , Lipid Peroxidation/drug effects , Male , Middle Aged , Neurodegenerative Diseases/blood , Neurodegenerative Diseases/enzymology , Neuroprotective Agents/therapeutic useABSTRACT
The kinetics of yeast hexokinase activity exposed to 1 MHz ultrasound of therapeutic intensities 0.1-1.5 W/cm2 was studied using traditional physico-chemical methods and by the thermoinactivation approach. Analysis of the kinetic curves and the kinetic parameters, obtained by two independent methods, suggested specific perturbation processes provoked by the ultrasonic waves, viz., the mechanical breakdown of the contact site between monomer units and the subsequent sonochemical modification of the active enzyme site. Low intensity ultrasound also caused the destabilization of the molecular structure of hexokinase as revealed by the apparent thermolability of the sonicated enzyme.
Subject(s)
Hexokinase/metabolism , Saccharomyces cerevisiae/enzymology , Ultrasonics , Kinetics , Protein Denaturation , TemperatureABSTRACT
Kinetics of erythrocyte acetylcholinesterase activity alterations exposed to ultrasound of therapeutic intensities of 0.88 MHz and 0.05-1.5 W/cm2 was studied. The differences were studied between the mechanisms of the inactivation of membrane-bound and free enzyme: the diminution of active enzyme sites for membrane-bound acetylcholinesterase and the decrease of enzyme-substrate affinity for the free form during sonication. The combined mechanical stresses in the ultrasonic field did not produce inactivation of free enzyme, as compared to the membrane-bound enzyme. Exponential ultrasonic/acoustochemical inactivation curves were obtained for the soluted crystalline form of acetylcholinesterase.
