324
Views
4
CrossRef citations to date
0
Altmetric
Research Article

Triton X-100 inhibition of yeast plasma membrane associated NADH-dependent redox activities

, &
Pages 205-209 | Received 03 Jun 2004, Accepted 08 Oct 2004, Published online: 03 Oct 2008

References

  • Crane FL, Barr R. Plasma membrane oxidoreductases. Crit Rev Plant Sci 1989;8:273–307.
  • Barr R, Bo¨ ttger M, Crane FL, Morre DJ. Electron donation to the plasma membrane redox system of cultured carrot cells stimulates Hþ release. Biochim Biophys Acta 1990;1017:91–95.
  • Misra PC. Transplasma membrane electron transport in plants. J Bioenerg Biomemb 1991;23:425–442.
  • Brightman AO, Barr R, Crane FL, Morre DJ. Auxin stimulated NADH oxidase purified from plasma membranes of soybean. Plant Physiol 1988;86:1264–1269.
  • Møller IM, Crane FL. Redox processes in the plasma membrane. In: Larsson C, Møller IM, editors. The Plant Plasma Membrane: Structure, Function and Molecular Biology. Berlin: Springer-Verlag; 1990. p 93–126.
  • Rubinstein B, Luster DG. Plasma membrane redox activity: Components and role in plant processes. Annu Rev Plant Physiol Plant Mol Biol 1993;44:131–155.
  • Crane FL, Roberts H, Linnane AW, Low H. Transmembrane ferricyanide reduction by cells of the yeast Saccharomyces cerevisiae. J Bioenerg Biomemb 1982;14:191–205.
  • Yamashoji S, Kajimoto G. Catalytic action of vitamin K3 on ferricyanide reduction by yeast cells. Biochim Biophys Acta 1986;849:223–228.
  • Yamashoji S, Kajimoto G. Decrease of NADH in yeast cells by external ferricyanide. Biochim Biophys Acta 1986;852:25–29.
  • Barr R. The possible role of redox associated protons in growth of plant cells. J Bioenerg Biomemb 1991;23:443–467.
  • Misra PC, Awasthi V. Modulation of plasma membrane Hþ- ATPase activity by transplasma membrane electron transport in plants. Abstract No SX7. 67th Annual meeting of Society Biological Chemists (India), New Delhi, 1998.
  • Ismet SA, Tvaradze E, Kalilov RI. Abstract No. P21. Fifth International Conference on Plasma Membrane Redox System and their Role in Biological Stress and Disease, Hamburg, 2000.
  • Awasthi D, Awasthi V, Misra PC. Concanavalin A induced activity change in yeast PM-bound NADH-HCF(III) oxido- reductase. Biochim Biophys Acta 2004;1672:21–26.
  • Ulaszewski S, Grenson M, Goffeaue A. Modified plasma membrane ATPase in mutants of Saccharomyces cerevisiae. Eur J Biochem 1983;130:235–239.
  • Awasthi V, Misra PC. Interference in yeast plasma membrane protein estimation by percoll. Anal Biochem 2001;294:83–87.
  • Mauersberger S, Ohkuma M, Schunck W-H, Takagi M. Candida maltosa. In: Wolf K, editor. Non-Conventional Yeast in Biotechnology. Berlin: Springer-Verlag; 1996. p 411–580.
  • Delhez J, Dufour JP, Thines D, Goffeaue A. Comparison of the properties of plasma membrane bound and mitochondria bound ATPase in the yeast Schizosaccharomyces pombe. Eur J Biochem 1977;79:319–328.
  • Fiske CH, Subbarow Y. Determination of inorganic phos- phates. J Biol Chem 1925;66:375–400.
  • Morre DJ, Brightman AO, Wu L-Y, Barr R, Leak B, Crane FL. Role of plasma membrane redox activities in elongation growth in plants. Physiol Plant 1988;73:187–193.
  • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein- dye binding. Anal Biochem 1976; 72:248–254.
  • Sandstrom RP, Cleland RE. Selective delipidation by surfactant: Enrichment of sterols and activation of ATPase. Plant Physiol 1989;90:1524–1531.
  • Ibarz E, Palmgren MG, Palazon J, Pinol M-T, Serrano R. Activation of plant plasma membrane Hþ- ATPase activity by nonionic detergent Brij-58. Biochim Biophys Acta 1994; 1196:93–96.
  • Barr R, Sandelius AS, Crane FL, Morre DJ. Oxidation of reduced nucleotides by plasma membrane of soybean hypocotyls. Biochem Biophys Res Commun 1985; 131:943–948.
  • Helenius A, Mc Caslin DR, Fries E, Tanford C. Properties of detergents. Methods Enzymol 1979;56:734–749.
  • Askerlund P, Larsson C, Widel S. Localization of donor and acceptor sites of NADH dehydrogenase activities inside-out and right side-out plasma membrane vesicles from plants. FEBS Lett 1988;239:23–28.
  • Szabo-Nagy A, Erdei L. The effects of iron deficiency on the ATPase and ferricyanide reductase activities of plasma membrane purified by phase partitioning from sunflower roots. J Plant Physiol 1993;142:563–584.
  • Lawrence K, Bhalla P, Misra PC. NADH-dependent redox activities on the external face of plasma membrane vesicles of chickpea roots. J Plant Physiol 1995;146:763–765.
  • Klobus J, Buczek J. The role of plasma membrane oxidoreductase activity in proton transport. J Plant Physiol 1995;146:103–107.
  • Gutman M. Effect of Triton X-100 on mitochondrial NADH dehydrogenase. Physiol Chem Phys 1970;2:9–14.
  • Bough RF, King TE. Purification, properties and reconstitu- tive activity of DPNH dehydrogenase. Biochem Biophys Res Commun 1972;49:1165–1173.
  • Ushakova AV, Grivennikova VG, Ohnishi T, Vinogradov AD. Triton X-100 as a specific inhibitor of the mammalian NADH- ubiquinone oxidoreductase (complex 1). Biochim Biophys Acta 1999;1409:143–153.
  • Okun JG, Zickermann V, Zwicker K, Scha¨gger H, Brandt U. Binding of detergents of inhibitor to bovine complex 1—a noval purification procedure for bovine complex 1 retaining full inhibitor sensitivity. Biochim Biophys Acta 2000;1459:77-87. [33] McGovern SL, Helfand BT, Feng B, Shoichet BK. A specific mechanism of nonspecific inhibition. J Med Chem 2003; 46:4265–4272.
  • Kreibich D, Sabatini P. Procedure for the selective release of content from microsomal vesicles without membrane disas- sembly. Methods Enzymol 1974;31:215–225.
  • Dixon M. The determination of enzyme inhibitor constants. Biochem J 1953;55:170–171.
  • Chang S-Y, Ko TP, Liang P-H, Wang AH-J. Catlytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium and Triton. J Biol Chem 2003;278:29298–29307.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.