PubMed Health⌕ Search

Biomedical subjects

V G Artiukhov

Publications and source records attributed to V G Artiukhov.

At least 19 recordsLinked to original sources
PubMed1990

[The oxygen-binding properties of hemoglobin modified by the action of temperature and sodium dodecyl sulfate].

Oxygen-binding properties of mice hemoglobin modified by temperature (20-45 degrees C) or by this temperature together with sodium dodecyl sulphate (SDS) of different concentrations (3.47 x 10(-5)-3.47 x 10(-4) M) were studied by means of spectrophotometry. The increase of temperature up to 42-45 degrees C resulted in accumulation of the hemoglobin aggregates larger than tetramers. The combined effect of SDS and temperature may change the protein microenvironment as well as to integrate the hemoprotein molecules into subunits, depending upon the SDS concentration.

Animals↗
PubMed1989

[Autologous transfusion of UV-irradiated blood in the treatment of occlusive arterial diseases of the lower extremities].

Complex examination of 72 patients with obliterating atherosclerosis and 10 patients with obliterating endarteritis was performed. All the patients were given autotransfusion of UV-irradiated blood as conservative treatment, preoperative preparation and postoperative management. The course of AUVIB was followed by a decrease of the lactic acid level, increase of functional properties of hemoglobin, activation of humoral immunity, change of the blood hemostatic potential to the side of hypocoagulation. The AUVIB treatment was most effective in patients at initial stages and those with peripheral forms of the disease.

Acid-Base Equilibrium↗
PubMed1983

[Protective action of serotonin in relation to oxyhemoglobin during the ultraviolet irradiation of a mixture of their solutions].

It was shown by the spectral method that 5 x 10(-5) serotonin protected native (20 degrees C) oxyhemoglobin (1,48 x 10(-5) M) against UV-irradiation of the mixture (dose 12,4 x 10(4) erg/sm2). Serotonin also displays the protective effect with thermally modified (45 degrees) hemoprotein as the degree photooxidation of oxyhemoglobin reduces in the presence of the radioprotective agent. The cause of the radioprotective effect is attributed to the formation of a serotonin-oxyhemoglobin complex.

Animals↗
PubMedDate not supplied

[UV-induced changes of structural and functional properties of blood lactate dehydrogenase isoenzymes in free state and in the presence of serotonin].

Photoinduced changes of structural and functional properties of lactatedehydrogenase isoenzymes from human erythrocytes in free state and in the presence of serotonin have been studied by means of gel chromatography, electrophoresis, IR-spectrophotometry and by the method of definition of catalytic activity. UV-light influence induces photoinactivation of erythrocyte's LDH, while its inhibitory effect intensifies with the increase of irradiation dose. The complicated character of changes in electrophoretic mobility and percentage content of isoenzymes LDH-1, LDH-2, LDH-3 under the influence of UV-rays testifies that the decrease of total enzyme activity of these isoforms in connected with their different photosensitiveness and represents the result of many-staged process which is characterized both by the consistent and parallel proceeding of its individual photochemical reactions. A pronounced photoprotective effect of serotonin towards the molecules of erythrocytic LDH isoenzymes has been discovered. It seems to be caused by formation of enzyme--biogenous amine complex affecting the secondary protein structure.

Animals↗
PubMedDate not supplied

[Regularities in the kinetic of photoactivation of lactate dehydrogenase by the action of UV light in different microenvironment].

The kinetics of photoinactivation of cardiac (H4) and muscular (M4) isoforms of lactate dehydrogenase irradiated by UV light (240-390 nm) in the free form and in the presence of sodium azide, D-mannitol, and serotonin was studied. It was shown that the decrease in the catalytic activity of both enzymes can be described by the kinetics of the first-order monomolecular reaction. The inactivation rate constant of lactate dehydrogenase M4 is considerably higher than that of lactate dehydrogenase H4, indicating a greater photochemical lability of the isoform M4. It was shown that sodium azide has a different protective action on the proteins studied. The irradiation of the muscular isoform in the presence of serotonin and D-mannitol did not change the character of the "dose-effect" curve and only led to a decrease in the photoinactivation rate constant of the protein.

Animals↗
PubMedDate not supplied

[An assessment of the degree of chromophore photo damage to the heme and globin components in UV-irradiated molecules and electrophoretic fractions of human carboxyhemoglobin].

The contribution of hem and globin components of electrophoretic fractions of UV-irradiated human carboxyhemoglobin to photodestruction of the protein was studied. The changes observed are the result of summation of some processes unequal in intensity and direction that take place in microheterogeneous media of photomodified protein. Photosensitivity of hemoproteid in electrophoretic fraction depends on apoprotein condition, whereas the hem photoresistance cannot be the evidence of the photostability of the whole molecule.

Blood Protein Electrophoresis↗
PubMedDate not supplied

[Oligomeric proteins: modulation of UV-sensitivity and characteristics of photochemical transformations].

The results of our research devoted to the study of photophysical and photochemical transformations of some compound proteins of oxidative, antioxidant, transport and immune systems of an organism under conditions of different microenvironment (presence of chemical modificators, the change of pH, temperature, doses and spectral composition of ultraviolet irradiation) have been analyzed. Methods and the degree of modulation of UV-sensitivity of proteins of the mentioned systems have been discussed. Conditions, on which the used chemical agents show photoprotective and photosensitizing effect on protein molecules, have been found.

Photochemistry↗
PubMedDate not supplied

[UV-sensitivity of hemoglobin dimers in free state and in valency hybrids: modification by serotonin]].

Changes of oxygen-binding activity of hemoglobin dimers modified by the therapeutical doses of UV-light and serotonin in free state and in valency hybrids are analyzed. The prior role of photodissociation to dimers at the UV-radiation action on heme-protein molecules has been shown. It has been observed that the complex between hemoglobin and serotonin is formed in fields of alpha beta-dimers contacts.

Dimerization↗
PubMedDate not supplied

[Structure-functional modification of lactate dehydrogenase isoforms under the effect of ultraviolet radiation and active forms of oxygen].

The investigation results on the UV-induced changes of lactate dehydrogenase structural and functional properties in the presence of some chemical substances, which are able to interact with the oxygen active forms have been summarized. As well the kinetic characteristics of the photoinactivation processes for heart and muscle LDH types in free state and in the complex with the exogenous agents have been studied. Singlet molecular oxygen has been shown to play an important role in the process of UV-modification of different protein isoforms. The scheme of probable physical and chemical processes, leading to the inactivation of lactate dehydrogenase molecules, has been suggested.

Isoenzymes↗
PubMedDate not supplied

[Effects of low intensity laser (632.8 nm) and ultraviolet radiation on spectral properties and functional activity of human ceruloplasmin].

Photoinduced changes of human ceruloplasmin (hCp) under laser and ultraviolet (UV) radiation have been studied. A complex character of hCp spectral modifications points to a different degree of the protein molecule folding. After the influence of UV radiation (240-390 nm) in a dose range 906-4530 J/m2 the decrease of oxidase hCp activity was registered. These changes are thought to be connected with modification of the conformation of hCp active centre or copper reduction that was confirmed by the decrease of optical density at 610 nm. An inactivation constant (kf = 3.8 x 10(-4) 1/s) and a photoinactivation quantum yield (1.4 x 10(-4)) were calculated. Kinetic dependencies of o-phenilen-diamine oxidation by intact and UV-modified glycoprotein do not correspond to Michaelis-Menten equation. UV radiation in a dose range 151-4530 J/m2 induced increasing of ceruloplasmin superoxiddismutase activity. The influence of He-Ne laser radiation (1.3 mW; lambda = 632.8 nm, exposure time from 1 up to 30 min) leads to the raise of the hCp functional activity; superoxiddismutase activity changes more significantly. Possible photophysical and photochemical processes in hCp molecule, leading to photomodification and changes of protein functional activity have been represented on the scheme.

Ceruloplasmin↗