These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Formation of lactate dehydrogenase complexes with proteins and polyelectrolytes. A possible physiological role].
    Author: Tsygankov AIu, Motorin IuA, Dobrushkin AE, Vol'fson AD, Orlovskiĭ AF.
    Journal: Biokhimiia; 1986 Apr; 51(4):590-5. PubMed ID: 3708013.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]