Abstract
Anionic [Na deoxycholate (DOC), Na cetyl sulfonate, Na lauryl sulfate, Na dodecyl benzene sulfonate], cationic (cetavlon, cetyldimethylbenzylammonium chloride, laurylamine) and nonionic detergents (Lubrol W and Tween 80) have different effects upon esterase and glucose-6-phosphatase (G-6-Pase) activities of mouse liver microsomes. The anionic and nonionic detergents solubilize esterase activity and microsomal proteins whereas the cationic ones partially inactivate and do not solubilize this enzyme or appreciable amounts of protein. G-6-Pase is activated by Lubrol W and DOC, is inactivated partially or completely by the other anionic detergents, but is less inactivated by the cationic detergents than is esterase. The solubilization of esterase but not G-6-Pase by the various detergents suggests that these enzymes probably have different sites in or on the microsomal membranes, or that one, esterase, is loosely bound and the other, G-6-Pase, is tightly associated with the microsomal membranes. The anionic detergent DOC and the nonionic detergent Lubrol W are able to protect to a limited extent and to a greater extent, respectively, esterase from the inactivating effect of cetavlon and of Na lauryl sulfate. This may be due to the preferential adsorption of DOC and Lubrol W to the esterase site on the microsomes, removal of which requires a fairly high concentration of the cationic detergent, cetavlon, or of Na lauryl sulfate.
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