[Lysosomal glycosidases, lactate dehydrogenase and creatine phosphokinase in experimental inflammation]. / Nekotorye lizosomal'nye glikozoidazy, laktatdegidrogenaza i kreatinfosfokinaza pri éksperimental'nom vospalenii.

Inflammation of rat hypodermic tissue was accompanied by an increase in activity of lysosomal glycosidases beta-D-galactosidase and beta-D-glucuronidase in the proliferating tissue and in some other preparations studied. Activation of lactate dehydrogenase/LDH/in exudate of inflamed tissues indicated apparently that the rate of redox reactions was elevated under conditions of the tissue proliferation. Decrease of creatine phosphokinase activity in blood plasma of experimental animals, which occurred simultaneously with the LDH activation, enabled to suggest the presence of compensatory mechanisms responsible for energy providing of the tissue proliferation.

[Partial purification and properties of the adenylate deaminase from subfractions of soluble mitochondrial proteins of rat liver]. / Chastichnaia ochistka i svoistva adenilatdezaminazy iz subfraktsii rastvorimykh mitokhondrial'nykh belkov pecheni krys.

Isolation and partial purification of AMP-deaminase from subfraction of soluble proteins of the mitochondrial fraction from rat liver is described. The enzyme preparations obtained deaminated AMP at the highest rate from pH 6.4 to 6.6. At the optimal pH value and in presence of optimal AMP concentrations the AMP-deaminase preparation was not activated by ATP or K+ and was inhibited by inorganic phosphate. Relationship was noted between both the content of protein in the enzyme preparations and length of the interval from composing the samples to monitoring the enzymatic activity and the following parameters of the AMP-deaminase: (a) shape of curves describing the rate of AMP deamination as a function of the nucleotide concentration, (b) reversible decrease in the AMP-deaminating activity after dialysis, (c) properties to deaminate, besides AMP, also some other nucleotides (ADP, NAD, FAD), (d) dynamics of inactivation of the enzyme preparations by controlled heating. The properties of the partially purified AMP-deaminase from the subfraction of rat liver soluble mitochondrial proteins were not identical with those described previously for other AMP-deaminases.

[Activity of various intracellular hydrolases in experimental inflammation]. / Aktivnost' nekotorynkh vnutrikletochnykh gidrolaz v dinamike éksperimental'nogo vospaleniia.

Activity of lysosomal hydrolases, cathepsins A and D, acid phosphatase, was induced in inflamed rat hypodermic tissue. Simultaneously, cytoplasmic enzymes leucine amino-peptidase and alkaline phosphatase were activated in the tissue. At the same time, activity of thiol-dependent enzymes/cathepsins B and C/ was decreased in all preparations studied. The data obtained suggest that both lysosomal and membrane-bound hydrolases participated in development of inflammation. Besides, proliferation of the hypodermic tissue appears to effect, by means of mediator and metabolite systems, on activity of intracellular enzymes in other tissues studied, which were not related directly to the impairment.

[Adenylate deaminase of the liver mitochondria in normal state and in alcoholic intoxication]. / O mitokhondrial'nykh adenillatdezaminazakh pecheni v norme i pri alkogol'noi intoksikatsii

AMP-deaminases were isolated and partially purified from subfractions of soluble mitochondrial proteins of rat liver under normal conditions and in ethanol intoxication. Repeated freezing and thawing of the mitochondrial fractions from liver of rats, which were treated with ethanol (1 ml of 32% solution daily for 7 days, intraperitoneally), liberated into the subfraction of soluble mitochondrial proteins significantly less AMP-deaminases, as compared with the control animals. The enzyme preparations obtained from intoxicated and intact animals were quite similarly inactivated by controlled heating, deaminated at similar rates AMP, ADP, FAD and some other nitrogenous compounds (but did not deaminate adenosine and some structural analogues of AMP). However, an inhibitory effect of the structural analogues of AMP and of nucleosides was significantly higher towards the AMP-deaminase from healthy rats as compared with the corresponding enzyme preparations obtained from the ethanol-treated animals. The increase in velocity of enzymatic AMP deamination in the subfraction of soluble mitochondrial proteins apparently does not represent a suitable target for possible therapeutic approaches to control the phenomenon, observed in the experimental ethanol intoxication, of stimulation of the deaminating activity in total mitochondrial fraction of rat liver.

[Monoamine oxidase and adenylate deaminase activity of mitochondrial fractions of the rat liver in alcoholic intoxication]. / Monoaminoksidaznaia i adenilatdezaminaznaia aktivnost' mitokhondrialhnykh fraktsii pecheni krys pri alkogol'noí intoksikats ii

Decrease in monoamine oxidase and increase in diamine oxidase and adenylate deaminating activities were found in rat liver mitochondrial fractions after repeated injections of ethanol. A monoamine oxidase inhibitor pargyline and an inhibitor of phosphodiesterase theophylline prevented the increase in adenylate deaminating activity in a subfraction of mitochondrial membranes in the ethanol intoxicated rats. In a subfraction of soluble mitochondrial proteins pargyline did not affect but theophylline prevented completely the increase in adenylate deaminating activity. The stimulation of adenylate deaminating activity in mitochondrial fractions of rat liver in ethanol intoxication might be caused by: 1) transformation of mitochondrial monoamine oxidases (in the subfraction of mitochondrial membranes) and 2) activation (or increased biosynthesis) of the adenylate deaminase in the subfraction of soluble mitochondrial proteins. The adenylate cyclase system is probably involved in the latter process.