Influence of polyethylene glycol on lactate dehydrogenase.
It is well established that polyethylene glycol (PEG) shifts the equilibrium in oligomeric protein systems to form higher molecular weight associates. We used this effect of PEG to evaluate a modification of functional properties of LDH from pig skeletal muscles. PEG decreases the rate of heating-induced LDH inactivation in the concentration dependent manner. Michaelis constant and maximal velocity of the enzyme as well as inhibition of LDH by high pyruvate concentrations were affected by PEG. Enzyme preincubation with PEG suppresses also the formation of ternary inactive complex NAD-pyruvate-LDH.
Lushchak
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Karadag Branch of Southern Sea Biology Institute, National Academy of Sciences of Ukraine, Crimea, Ukraine. lushchak@karadag.crimea.ua
D000818:Animals; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006358:Hot Temperature; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000201:enzymology; D009243:NAD / Q000737:chemistry; D011092:Polyethylene Glycols / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects; D019289:Pyruvic Acid / Q000737:chemistry / Q000494:pharmacology; D013552:Swine
D004791:Enzyme Inhibitors; D009243:NAD; D011092:Polyethylene Glycols; D019289:Pyruvic Acid; D007770:L-Lactate Dehydrogenase