[Structure-functional modification of lactate dehydrogenase isoforms under the effect of ultraviolet radiation and active forms of oxygen]. / Strukturno-funktsional'nye modifikatsii izoform laktatdegidrogenazy pod vliianiem UF-oblucheniia i aktivnykh form kisloroda.

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.

[Regularities in the kinetic of photoactivation of lactate dehydrogenase by the action of UV light in different microenvironment]. / Kineticheskie zakonomernosti fotoaktivatsii laktatdegidrogenazy pod deistviem UF-izlucheniia v usloviiakh razlichnogo mikrookruzheniia.

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.

[Active forms of oxygen and the degree of UV modification of the structural and functional properties of lactate dehydrogenase]. / Aktivnye formy kisloroda i stepen' UF-modifikatsii strukturno-funktsional'nykh svoistv laktatdegidrogenazy.

The spectrophotometry and photofluorescence techniques were used in the studies on photochemical transformations of lactate dehydrogenase exposed to UV irradiation with a dose of 2.25 kJ/m2, in the native state and in the presence of exogenous modifiers: sodium azide, beta-carotene, histidine, D-mannitol, and tret-butanol. It was shown that UV irradiation of the mixtures of lactate dehydrogenase with sodium azide, beta-carotene, and histidine results in restoration (by 99, 65, and 63%, respectively) of the level of catalytic activity of the enzyme as compared to that observed after irradiating it in the absence of the protectors. The protective effect provided by mannitol during UV irradiation of the lactate dehydrogenase was 23%. Thus, it was shown that active oxygen species--singlet molecular oxygen and hydroxyl radical--make significant contributions to photomodification of lactate dehydrogenase.