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A. Liberman, S. A. Ostroumov, V. D. Samuilov, A. Yu. Semenov, and V. P. Skulachev, Bioorg. Khim. l, 113 (1975). 3 L. A. Drachev, V. N. Frolov, A. D. Kaulen, E. A. Liberman, S. A. Ostroumov, V. G. Plakunova, A. Yu. Semenov, and V. P. Skulachev, J. Biol. Chem. 251, 7059 (1976). 4 V. P. Skulachev, FEBS Lett. 64, 23 (1976). 5 L. A. Drachev, A. D. Kaulen, A. Yu. Semenov, I. I. Severina, and V. P. Skulachev, Anal. Biochem. 96, 250 (1979). 6 V. P. Skulachev, this series, Vol. 55, pp. 586 and 751. METHODS IN ENZYMOLOGY,VOL, 88 Copyright© 1982by AcademicPress, Inc.

N. Ames and D. T. Dubin, J. Biol. Chem. 235, 769 (1960). 6 M. Rehorek and M. P. Heyn, Biochemistry 18, 4977 (1979). E. F. Hartree, Anal. Biochem. 48, 422 (1972). W. A. Petri, Jr. and R. R. Wagner, J. Biol. Chem. 254, 4313 (1979). 9 V. H. Engelhard, B. C. Guild, A. Helenius, C. Terhorst, and J. L. Strominger, Proc. Natl. Acad. Sci. A. 75, 3230 (1978). 10 A. Helenius, E. Fries, and J. Kartenbeck, J. Cell Biol. 75, 866 (1977). 34 BACTERIORHODOPSIN [6] radii varying between 100 and 300 nm. 1 Similar values for the average radius were obtained from quasi-elastic light scattering.

Heyn, FEBS Lett. 108, 307 (1979). 3 N. A. Dencherand M. P. Heyn, FEBS Lett. 96, 322 (1978). 4 N. A. Dencherand M. P. Heyn, this volume, Article [2]. METHODS IN ENZYMOLOGY, VOL. 88 Copyright © 1982by Academic Press, Inc. All rights of reproduction in any form reserved. ISBN 0-12-181988-4 32 BACTERIORI-[ODOPSIN [6] lipid film comes off the bottom of the flask. The mixture is kept in the water bath at the required temperature for 10 min more with occasional shaking. Since bacteriorhodopsin solubilized in octyl glucoside is light sensitive, 3 the flask is protected from light by aluminum foil.

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