CLINICAL, INSTRUMENTAL AND BIOCHEMICAL ASSOCIATIONS OF THE DEGREE OF PHYSICAL RECOVERY IN PATIENTS SUFFERED FROM ACUTE CORONARY SYNDROME AT THE COMPLETION OF IN-HOSPITAL REHABILITATION PERIOD.

Objective: The aim: To determine the clinical, instrumental and biochemical factors associated with the degree of physical recovery in patients suffered from acute coronary syndrome (ACS) at the completion of in-hospital rehabilitation period.

Patients And Methods: Materials and methods: We enrolled 88 patients (all were males); 77 patients had ACS/STEMI and 11 with ACS/unstable angina. The mean age was (median, interquartile range) was 58 (49-64) years.

[Interaction between 5-lipoxygenase and allosteric effector--sodium dodecyl sulfate].

The role of allosteric effector--sodium dodecyl sulfate (SDS) in the lipoxygenase catalysis in micelle system has been studied. The effect of the stable hydrophobic bis-nitroxides, blocking the free radical transformation, on the oxidation of linoleic acid or linoleic alcohol by 5-lipoxygenase from potato tuber has been investigated. The inhibiting effect of nitroxide compounds on oxidation of linoleic acid or linoleic alcohol by 5-lipoxygenase depends on SDS concentration.

[Inhibiting properties of stable nitroxyl radicals in reactions of linoleic acid and linoleyl alcohol oxidation catalyzed by 5-lipoxygenase].

The inhibiting effects of 2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO) and its 4-substituted derivatives in reactions of linoleyl acid or linoleyl alcohol oxidation catalyzed by potato tuber 5-lipoxygenase were investigated. Inhibiting properties of stable nitroxyl radicals in presence of lubrol and SDS were reduced at the transition from TEMPO to 4-hydroxy-TEMPO or 4-amino-TEMPO and increased at use of adamantane-1-carboxylic or 3-methyladamantane-1-carboxylic acid 1-oxyl-2,2,6,6-tetramethylpiperidine-4-yl esters. Enzyme activity at saturating concentrations of inhibitor was not suppressed completely, and decreased up to the certain level determined by the substrate nature.

[Hydrophobic nitroxyl radicals inhibit linoleyl alcohol oxidation by 5-lipoxygenase].

The linoleyl alcohol oxidation catalyzed by potato tuber 5-lipoxygenase was found to be efficiently inhibited by stable nitroxyl radicals: 1-oxyl-2,2,6,6-tetramethylpiperidin-4-yl 1-bicyclo[2,2,2]octane-1-carboxylate, 1-adamantylacetate, dodecanoate, and octadecanoate. The dependence of apparent IC50 values on the rotational correlation times of times of 4-hydroxy-1-oxyl-2,2,6,6-tetramethylpiperidine and its derivatives in model micellar systems was analyzed. The inhibition mechanism was proposed; it involves the interaction of hydrophobic nitroxyl radical with the intermediate radical enzyme-substrate complex.

[Relative reactivity of thiamine monophosphate and thiamine diphosphate upon interaction with alkaline phosphatase].

Reactivity of thiamin monophosphate (TMP) as calf intestinal alkaline phosphatase substrate in model transformations is lower comparing with thiamin diphosphate (TDP) reactivity. Under these conditions alkaline phosphatase catalyzes TDP, ADP and AMP hydrolysis approximately at same rate. It was shown that TDP competes with p-nitrophenyl phosphate more effectively than TMP for the binding in the active site.