Esterase distribution in mouse liver
1961
Abstract About 80% of the esterase activity of mouse liver homogenized and fractionated in sucrose is found in the microsomes, and this distribution is independent of the sucrose concentration. The stability of the esterase activity of the microsomes is dependent upon the concentration of sucrose used for the isolation of these particulates, and greatest stability is found in microsomes isolated from 0.88 M sucrose. Esterase activity is distributed both in “rough-surfaced” and “smooth-surfaced” microsomal membranes, and nearly half of its activity is destroyed in these fractions following homogenization with glycerol, sucrose, and NaCl. The employment of sodium deoxycholate to dissolve the vesicular portion of the microsomes and ribonuclease to hydrolyze the ribonucleoprotein particles showed that the esterase activity of the microsomes is associated with, or is a part of the membranes or their contents. Very low concentrations of diethyl p -nitrophenyl phosphate and tetraethyl pyrophosphate, potent inhibitors of esterase activity, completely inhibit microsomal esterase activity, which activity appears to be of the B-type of Aldridge. No explanation could be found for the fact that the addition of glycerol to the fractionation media of liver cell particulates results in nearly half of the esterase activity being found in the supernatant fraction.
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