The role of lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies

• Autorzy: Terlecki G , Czapinska E. , Gutowicz J.
• Języki publikacji: EN

Abstrakty

EN

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 LDH, 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 the used concentration values did not alter the activity of the enzyme when it was used on its own, but did diminish 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.

Słowa kluczowe

EN

liposome; lactate dehydrogenase; cell membrane; enzyme-lipid interaction; enzyme; membrane; glycolytic enzyme; phosphatidylserine

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2002
• Tom: 07
• Numer: 3
• Opis fizyczny: p.895-903,fig.

Twórcy

autor

Terlecki G

• Wroclaw Medical University, Wroclaw, Poland

autor

Czapinska E.

autor

Gutowicz J.

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