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Tytuł oryginału: The role lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies.
Autorzy: Terlecki Grzegorz, Czapińska Elżbieta, Gutowicz Jan
Źródło: Cell. Mol. Biol. Lett. 2002: 7 (3) s.895-903, il., bibliogr. 27 poz.
Sygnatura GBL: 306,513

Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Streszczenie angielskie: Lactate dehydrogenase is one of the enzymes of the glycolytic path. It has been shown to be able to bind in vitro to cellular membranes. The presence of anionic phospholipids induces changes in the catalytic properties of the enzyme similar to those found when the enzyme is bound to natural membranes. In this study, a nonionic detergent (Tween 20), at concentrations not affecting the catalytic activity of LDL, was used to study the role of the lipid supra-molecular structure in the interaction between pig skeletal muscle lactate dehydrogenase and phosphatidylserine. Tween 20 changes the equilibrium of concentrations between the lipid supra-molecular forms. The detergent at ther used concentration values did not alter the activity of the enzyme when it was used on its own, but did diminsh the level of inhibition induced by the studied phospholipid. The obtained results showed that the interaction is reversible and that the bilayer structure of the lipid is essential for the inhibition.

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