[Effect of low-intensity 900 MHz frequency electromagnetic radiation on rat liver and blood serum enzyme activities].

The comparative analysis of the rat liver and blood serum creatine kinase, alanine aminotransferase, aspartate aminotransferase, alkaline phosphatase and purine nucleoside phosphorylase post-radiation activity levels after a total two-hour long single and fractional exposure of the animals to low-intensity 900 MHz frequency electromagnetic field showed that the most sensitive enzymes to the both schedules of radiation are the liver creatine kinase, as well as the blood serum creatine kinase and alkaline phosphatase. According to the comparative analysis of the dynamics of changes in the activity level of the liver and blood serum creatine kinase, alanine aminotransferase, aspartate aminotransferase and purine nucleoside phosphorylase, both single and fractional radiation schedules do not affect the permeability of a hepatocyte cell membrane, but rather cause changes in their energetic metabolism. The correlation analysis of the post-radiation activity level changes of the investigated enzymes did not reveal a clear relationship between them. The dynamics of post-radiation changes in the activity of investigated enzyme levels following a single and short-term fractional schedules of radiation did not differ essentially.

[Influence of ionizing radiation on enzymatic activity and state of nucleus-nucleolar apparatus in rat hepatocytes].

The effects of a single exposure of rats to the whole-body roentgen irradiation at the doses of 3.5 Gy and 4.5 Gy on the activity of creatine kinase, purine nucleoside phosphorylase, alanine aminotransferase, aspartate aminotransferase, as well as on the state of the nuclear-nucleolar apparatus in rat hepatocytes on the 6th and 13th days after radiation exposure have been studied. Irradiation at the above doses induced changes in the levels of enzymatic activity of different values and different directions within the same time periods, as well as oscillating changes in this type of enzymatic activity over time. This demonstrates various radiosensitivity and adaptation abilities of these enzymatic activities. The changes in the enzymatic activity significantly correspond to the changes in the morphometric indices of nuclear-nucleolar apparatus of hepatocytes, as well as the distribution of hepatocytes within the ploidy classes: in particular, stabilization of the enzymatic activity on the 13th day after irradiation correlates with the increased transcriptional activity, which is detectable through the increased number of nucleoli per nucleus and the expanded space of a hepatocyte nucleus. The compensation mechanisms are likely to be targeted at the changes in the functional activity of surviving hepatocytes, rather than at the replacement of the damaged cells by the new ones.

[Purine nucleoside phosphorylase].

Purine nucleoside phosphorylase (PNP) is one of the most important enzymes of the purine metabolism, wich promotes the recycling of purine bases. Nowadays is the actual to search for effective inhibitors of this enzyme which is necessary for creation T-cell immunodeficient status of the organism in the organs and tissues transplantation, and chemotherapy of a number pathologies as well. For their successful practical application necessary to conduct in-depth and comprehensive study of the enzyme, namely a structure, functions, and an affinity of the reaction mechanism. In the review the contemporary achievements in the study of PNP from various biological objects are presented. New data describing the structure of PNP are summarised and analysed. The physiological role of the enzyme is discussed. The enzyme basic reaction mechanisms and actions are considered. The studies on enzyme physicochemical, kinetic, and catalytic research are presented.

Constraints on the fundamental string coupling from B-mode experiments.

We study signatures of cosmic superstring networks containing strings of multiple tensions and Y junctions, on the cosmic microwave background (CMB) temperature and polarization spectra. Focusing on the crucial role of the string coupling constant g(s), we show that the number density and energy density of the scaling network are dominated by different types of string in the g(s) ~ 1 and g(s) ≪ 1 limits. This can lead to an observable shift in the position of the B-mode peak--a distinct signal leading to a direct constraint on g(s). We forecast the joint bounds on g(s) and the fundamental string tension µ(F) from upcoming and future CMB polarization experiments, as well as the signal to noise in detecting the difference between B-mode signals in the limiting cases of large and small g(s). We show that such a detectable shift is within reach of planned experiments.

[Some inhibitors of purine nucleoside phosphorylase].

Purine nucleoside phosphorylase (PNP) catalyzes reversible phosphorolysis of purine deoxy- and ribonucleosides with formation (d)Rib-1-P and corresponding bases. PNP plays a leading role in the cell metabolism of nucleosides and nucleotides, as well as in maintaining the immune status of an organism. The major aim of the majority of studies on the PNP is the detection of highly effective inhibitors of this enzyme, derivatives ofpurine nucleosides used in medicine as immunosuppressors, which are essential for creating selective T-cell immunodeficiency in a human body for organ and tissue transplantation. The present work is devoted to the study of the effects of some synthetic derivatives of purine nucleosides on activity of highly purified PNP from rabbit spleen and also from human healthy and tumor tissues of lung and kidneys. Purine nucleoside analogues modified at various positions of both the heterocyclic base and carbohydrate residues have been investigated. Several compounds, including 8-mercapto-acyclovir, 8-bromo-9-(3,4-hydroxy-butyl)guanine, which demonstrated potent PNP inhibition, could be offered for subsequent study as immunosuppressors during organ and tissue transplantation.

[Purine nucleoside phosphorylase inhibitors and their clinical significance].

PNP catalyzes a reversible phosphorolysis of purine deoxy- and ribonucleosides with formation of (d)Rib-1-P and appropriate bases. PNP plays a leading role in the cell metabolism of nucleosides and nucleotides, as well as in maintaining the immune status of an organism. The major purpose of the majority of studies on the PNP is the detection of high-performance enzyme inhibitors, derivatives of the purine nucleosides, which are used in medicine as immunosuppressors. It is well known that the latter are necessary for creating a selective T-cell immunodeficiency in a human body under organs and tissue transplantation. The review discusses the issues related to deliberate synthesis of effective, metabolically inert, and low-toxic PNP inhibitors. It also analyzes the available studies on substrate and inhibitory properties of the analogues of purine nucleosides, as well as research on the structural factors which reinforce the inhibitor activity of those analogues. The inhibitors which are either used in medical practice or are currently at a stage of preclinical testing are described. The inhibitors which are more efficient in their influence on the PNF from tumorous tissues are of special interest. Using PNP inhibitors in case of a number of pathologies denotes the importance and promise of research on both the enzyme and the compounds affecting its activity.