[Thermally-induced changes in structure-kinetic properties of lactate dehydrogenase].
Structural and functional properties of the lactate dehydrogenase modified by temperature at range 40-70 degrees C have been investigated. Kinetic principles of the thermoinactivation have been studied. The rate constants and the activation energy have been determined. Analysis of changes of the protein molecular mass leads to the conclusion that high-temperature denaturation of the lactate dehydrogenase (in investigated temperature interval) depends on oligomer molecule dissociation to monomers and subsequent aggregation of protein subunits.
Artiukhov
V G
VG
Nakvasina
M A
MA
Popova
V V
VV
D000818:Animals; D006358:Hot Temperature; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D013329:Structure-Activity Relationship; D013552:Swine
D007770:L-Lactate Dehydrogenase
Termoindutsirovannye izmeneniia strukturno-kineticheskikh svoĭstv laktatdegidrogenazy.