Abstract
THE property of water-insoluble amphipathic molecules to alter the electrokinetic charge of lipids has been exploited by Bangham and Dawson1 in elucidating the charge requirements of certain enzyme/substrate interactions. Their results show clearly the interdependence of both sign—positive or negative— and magnitude of enzyme and substrate interaction in any particular ionic environment. Whereas variation of pH, uni- or di-valent ion concentrations may affect the charge on both enzyme and substrate simultaneously, the addition of a water-insoluble amphipathic molecule to the lipid ensured an alteration of the substrate exclusively.
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References
Bangham, A. D., and Dawson, R. M. C., Biochem. J., 72, 486 (1959).
Poole, J. C. F., Robinson, D. S., and Macfarlane, R. G., Quart. J. Exp. Physiol., 40, 276 (1955).
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Bangham, A. D., Flemans, R., Heard, D. H., and Seaman, G. V. F., Nature, 182, 642 (1958).
Bell, W. N., and Alton, H. G., Nature, 174, 880 (1954).
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BANGHAM, A. A Correlation between Surface Charge and Coagulant Action of Phospholipids. Nature 192, 1197–1198 (1961). https://doi.org/10.1038/1921197a0
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DOI: https://doi.org/10.1038/1921197a0
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