[Formation of lactate dehydrogenase complexes with proteins and polyelectrolytes. A possible physiological role].
The effect of polymers (proteins, polyaminoacids, polyethylenimine) on kinetic parameters of lactate dehydrogenase (LDH) from porcine skeletal muscle was studied. Activation of the enzyme which was partially due to the association of LDH dimers was observed. A hypothesis was proposed, according to which the contribution of dissociation of oligomeric enzymes in the regulation of their activity in vivo is negligible due to the equilibrium shift towards association in dissociable enzyme systems.
A Iu
AIu
Tsygankov
Iu A
IuA
Motorin
A E
AE
Dobrushkin
A D
AD
Vol'fson
A F
AF
Orlovskiĭ
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D011108:Polymers / Q000032:analysis / Q000494:pharmacology*; D011485:Protein Binding; D011487:Protein Conformation; D013552:Swine
D001798:Blood Proteins; D046911:Macromolecular Substances; D011108:Polymers; D007770:L-Lactate Dehydrogenase
Obrazovanie kompleksov laktatdegidrogenazy s belkami i poliélektrolitami. Vozmozhnaia fiziologicheskaia rol'.