[Diagnostic significance of the determination of IgE in food allergy]. / Diagnosticheskoe znachenie opredeleniia immunoglobulina E pri pishchevoi allergii.

The total level of IgE was determined in 84 patients with food allergy and in 19 healthy individuals. The level of IgE was significantly elevated in food allergy reflecting a degree of body sensitization. The absence of complete correlation between the clinical signs of disease and the blood level of IgE could depend upon the involvement of IgG-mediated allergic reactions in the pathogenesis of disease. Specific antibodies to ovalbumin of the IgG class were detected in 18 of 25 patients. Certain correlation between a therapeutic clinical effect and the time course of the serum level of IgE was observed.

[Changes in the amine oxidase activity of human serum during different types of anesthesia and hyperbaric oxygenation]. / Izmenenie aktivnosti aminoksidaz syvorotki krovi cheloveka pri nekotorykh vidakh anestezii i pri giperbaricheskoo oksigenatsii.

Some types of anesthesia, used usually in labor anesthesia (sodium hydroxybutyrate, lexir) or in abdominal delivery (neuroleptanesthesia, cetalar narcosis, electroanesthesia) did not affect distinctly the activity of amine oxidases in blood sera of women in labor and of fetus. In some groups of women in labor the neonates were found, blood serum of which exhibited high activity of diamine oxidase, not observed in normal state. A slight decrease in deamination of benzylamine (20%) and 4-nitrobenzylamine (30%) was observed in patients with gynecological diseases within 2 and 3 days after operations. If intestinal paresis developed in the patients within the postoperational period deamination of these substrates was decreased by 75-80% in blood sera. After 2-4 courses of hyperbaric oxygenation a slight but statistically distinct decrease (by 22-25%) in the rate of deamination of benzylamine and 4-nitrobenzylamine was found in blood sera of the patients.

[Kinetics of the inhibition of mitochondrial monoamine oxidases A and B from rat liver by 1-(indolyl-3)isopropylmethylpropargylamine]. / Kinetika ingibirovaniia mitokhondrial'nykh monoaminoksidaz tipov A i B pecheni krysy 1-(indolil-3)izopropilmetilpropargilaminom.

The kinetics of inhibition of the activity of monoamine oxidases A (with 5-oxytryptamine as substrate) and B (with 2-phenylethylamine as substrate) from rat liver mitochondria by a new acetyleneamine, 1-(indolyl-3)isopropylmethylpropargylamine, was studied. It was shown that the inhibition of the both forms of monoamine oxidase results in formation of an intermediate dissociating enzyme--inhibitor complex which is further converted into an irreversibly blocked enzyme. The value of the dissociation constant, Ki, of the intermediate enzyme--inhibitor complex with 2-phenylethylamine as substrate is equal to 24 . 10(6) M, that with 5-oxytryptamine--to 0.09 . 10(-6) M. The values of the rate constants, K3, for the conversion of the enzyme--inhibitor complex into an irreversibly blocked enzyme in experiments with 2-phenylethylamine and 5-oxytryptamine were rather close, i. e. 0.06 and 0.05 min-1, respectively. The results obtained indicate that the selectivity and inhibition of the activity of monoamine oxidases A and B by propargylamine derivatives is manifested at the primary step of formation of dissociating intermediate enzyme--inhibitor complexes.

[Purification and properties of the serotonin-stimulated adenylate deaminase from the mitochondrial fraction of rat liver]. / Ob ochistke i svoistvakh stimuliruemoi serotoninom adenilatdezaminazy mitokhondrial'noi fraktsii pecheni krysy

A method is described for partial purification of structurally bound adenilate desaminase from rat liver tissue mitochondria; the enzyme was stimulated by parenteral administration of serotonine. The enzymatic preparations obtained desaminated AMP, 2',3'-AMP and adenosine, but they did not effect on ATP, 2',3'-cycloAMP or 3',5'-cycloAMP. The maximal rate of desaminating of these substances by AMP-desaminase, stimulated with serotonine, exceeded approximately 1.4-fold the same values, which were obtained for the enzymatic preparations from liver tissue mitochondria of rats, administered with physiological solution. Mitochondrial serotomine-stimulated adenilate desaminase was differentiated from the other soluble adenilate desaminases by some properties; the enzyme was likely to participate also in the regulation of nucleotides balance in the organism.

[Specificity and mechanism of serotonin stimulation of adenylate deaminase activity]. / O spetsifichnosti i mekhanizme stimuliatsii serotoninom adenilatdezaminaznoi aktivnosti

Adenylate deaminating activity was stimulated in the liver mitochondria of rats in vivo not only by serotonin or synthetic indolylalkylamines, but also by phenyl- and imidazolalkyamines. Actinomycin D and cycloheximide protein biosynthesis inhibitors prevented stimulation of adenylate deaminating activity. Theophylline, phosphodiesterase inhibitor, produced a similar effect only when the extent of stimulation of adenylate deaminating activity was comparatively high.

Stimulation of adenylate deaminase activity by serotonin.

After a single intraperitoneal injection of serotonin into rats adenylate deaminase activity in the mitochondrial fraction of the liver was stimulated. The conditions under which a twofold increase in the deamination of AMP occurred, after serotonin administration,were determined. Preliminary blocking of monamine oxidase activity did not prevent this effect of serotonin.