[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.
Artiukhov
V G
VG
Voronezh State University, Voronezh, Russia.
Nakvasina
M A
MA
Lysenko
Iu A
IuA
Agisheva
N V
NV
D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D017382:Reactive Oxygen Species; D013329:Structure-Activity Relationship; D014466:Ultraviolet Rays
D007527:Isoenzymes; D017382:Reactive Oxygen Species; D007770:L-Lactate Dehydrogenase