Abstract
Electrospray mass spectrometry (ESMS) of biological macromoleculeshas benefited from recent technical advances. Now it is feasible to observe the species injected at physiological pH and thus the mass determined has a direct relevance to these species present in solution (Ganem, et al., 1991, Cheng, et al., 1995). Intra- and intermolecular weak non-covalent interactions can now be determined (Smith and Light-Wahl, 1993).
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References
Cheng, X., Chen, R., Bruce, J.E., Schwarz, B.L., Anderson, G.A., Hofstadler, S.A., Gale, D.C., Smith, R.D., Gao, J., Sigal, G.B., Mammen, M. and Whitesides, G.M., Using Electrospray Ionisation FTICR Mass Spectrometry to Study Competive Binding of Inhibitors to Carbonic Anhydrase. (1995) J. Am. Chem. Soc. 117, 8859–8860.
Dvornik, D., (1987) Aldose Reductase Inhibition, Mc Graw-Hill, New York.
Ganem, B., Li, Y.T. and Henion, J.D., Detection of Noncovalent Receptor-Ligand Complexes by Mass Spectrometry. (1991) J. Am. Chem. Soc. 113, 6294–6296.
Pang Y.-P., Quiram P., Jelacic T. and Brimijoin, S., A Novel Strategy for Developing Potent and Selective Acetylcholinesterase Inhibitors. (1996) Jour. Biol. Chem., in press.
Reymann, J.M., Rondeau, J.M., Barth, P., Jaquinod, M., Van Dorsselaer, A. and Biellmann, J.F., Purification and electrospray mass spectrometry of aldose reductase from pig lens. (1992) Biochim. Biophys. Acta. 1122, 1–5.
Rondeau, J.M., Moras D., Tete, F., Podjarny, A., Dorsselaer, A. V., Reymann, J.-M., Barth, P. and Biellmann, J.F., Structural Studies of Pig Lens Aldose Reductase: Reversible Dimerisation of the Enzyme. (1991) in Enzymology and Molecular Biology of Carbonyl Metabolism 3, Weiner, H., Wermuth, B., Crabb, D. W., Ed. Plenum Press, New York, p 113–118.
Rondeau, J.M., Tête-Favier, F., Podjarny, A., Reymann, J.M., Barth, P., Biellmann, J.F. and Moras, D., Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. (1992) Nature, 355, 469–472.
Smith, R.D. and Light-Wahl, K.J., The observation of non-covalent interaction in solution by electrospray ionization mass spectrometry promise, pitfalls and prognosis. (1993) Biol. Mass Spectrom. 22, 493–501.
Wilson, D.K., Tarle, I., Petrash, J.M. and Quiocho, F.A., Refined 1.8 Angstrom structure of human aldose reductase complexed with the potent inhibitor zopolrestat. (1993) Proc. Natl. Sci. Acad. U.S.A., 90, 9847–9851.
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Potier, N., Barth, P., Tritsch, D., Biellmann, JF., Van Dorsselaer, A. (1996). Study of Non-Covalent Enzyme-Inhibitor Complexes of Aldose Reductase by Electrospray Mass Spectrometry. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_51
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_51
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