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2002 | 07 | 3 |
Tytuł artykułu

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

Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
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.
Wydawca
-
Rocznik
Tom
07
Numer
3
Opis fizyczny
p.905-910,fig.
Twórcy
autor
  • Wroclaw Academy of Medicine, Wroclaw, Poland
autor
Bibliografia
  • 1. Ehmann, J. D. and Hultin, H. O. Substrate inhibition of soluble and bound lactate dehydrogenase (isoenzyme 5). Arch. Biochem. Biophys. 154 (1973) 471-475.
  • 2. Dąbrowska, A., Gutowicz, J. and Terlecki, G. Adsorption of bovine muscle lactate dehydrogenase to erythrocyte membranes. Gen. Physiol. Biophys. 9 (1990) 529-534.
  • 3. Esakova, T. V. and Ivanov, M. V. Lactate dehydrogenase binding to sarcoplasmic reticulum membranes. Biokhimiia 57 (1992) 253-266.
  • 4. Volker, W. and Knull, H. R. A glycolytic enzyme binding domain on tubulin. Arch. Biochem Biophys. 338 (1997) 237-243.
  • 5. Karkhoff-Schweizer, R. and Knull, H. R. Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach. Biochem. Biophys. Res. Commun. 146 (1987) 827-831.
  • 6. Dąbrowska, A. and Gutowicz, J. Interaction of bovine muscle latate dehydrogenase with erythrocyte lipids. Biochim. Biophys. Acta 855 (1986) 99-104.
  • 7. Dąbrowska, A., Terlecki, G. and Gutowicz, J. Interaction of bovine skeletal muscle lactate dehydrogenase with liposomes. Comparison with the data for the heart enzyme. Biochim. Biophys. Acta 980 (1989) 357-360.
  • 8. Dąbrowska, A., Terlecki, G., Czapińska, E. and Gutowicz, J. Interaction of bovine heart pyruvate kinase with phospholipids. Biochim. Biophys. Acta 1236 (1995) 299-305.
  • 9. Gutowicz, J. and Modrzycka, T. Liposome-interaction induced conformation changes of glyceraldehyde-3-phosphate dehydrogenase. Gen. Physiol. Biophys. 5 (1986) 297-306.
  • 10. Gutowicz, J. and Kosmider-Schmidt, A. Fluorescence investigation on conformational state of rabbit muscle aldolase interacting with phsphatidylinositol liposomes. Biophys. Chem. 27 (1987) 97-102.
  • 11. Terlecki, G., Czapińska, E. and Gutowicz, J. The role of lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies. Cell. Mol. Biol. Lett. 7 (2002) 895-903.
  • 12. Lakowicz, J. Factors affecting the emission spectra of proteins in Principles of fluorescence spectroscopy. (Lakowicz, J. Ed.) Plenum Press, New York and London, 1983, 354-363.
  • 13. Tsuji, S., Quereshi, M. A, Hou, E. W., Fich, W. M. and Li, S. S. Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals, birds, an amphibian, fish, barley, and bacteria: cDNA sequences from Xenopus, pig, and rat. Proc. Natl. Acad. Sci. USA 91 (1994) 9392-9396.
  • 14. Burstein, E. A., Vendenkina, N. S. and Ivkova, M. N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18 (1973) 263-279.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-a5b64beb-e9f7-4817-b305-fb9f2bb67ae1
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