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Further evidence for the importance of lipid bilayers in the interaction between lactate dehydrogenase and phosphatidylserine

100%

Terlecki G., Gutowicz J.

Cellular and Molecular Biology Letters

2002

tom 07

nr 3

Lactate dehydrogenase (LDH) is one of the glycolytic enzymes, which have been proved to have the capability to reverse non-specific adsorption on cellular membranous structures in vitro, as well as on the structural proteins of the contractile system of muscle cells. It has been suggested that this binding may play a physiological role, as it alters the enzyme’s kinetic properties. Our previous studies on this enzyme showed that its interaction with some anionic phospholipids reveals similar characteristics and similar effect on the activity of the enzyme to those wich had been observed for the interaction with membranous structures. Disruption of the lipid bilayers by nonionic detergent (Tween 20) restored the enzyme activity inhibited by the presence of phosphatidylserine (PS) liposomes. In this study, we used the measurement of enzyme tryptophanyl fluorescence spectra to monitor the interaction and possible changes in the enzyme conformation. The investigation provided further evidence of the importance of the bilayer structure in this interaction. Similarly to the effect on the activity of the enzyme, the addition of Tween 20 diminishes the quenching of the LDH tryptophanyl ﬂuorescence, and finally completely restores the fluorescence.

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

84%

Terlecki G., Czapinska E., Gutowicz J.

Cellular and Molecular Biology Letters

2002

tom 07

nr 3

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.

Ograniczanie wyników

2 Cellular and Molecular Biology Letters

2 Gutowicz J.

2 Terlecki G.

1 Czapinska E.

2 2002

Wyniki wyszukiwania

Further evidence for the importance of lipid bilayers in the interaction between lactate dehydrogenase and phosphatidylserine

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