Homogenates of liver from cases of hepatic cirrhosis due to α(1)-antitrypsin deficiency(Pp) and alcoholism were analyzed for their content of various lysosomal enzymes. Also determined were the specific activities of lactate dehydrogenase, glutamate-oxaloacetate transaminase, glutamate-pyruvate transaminase, and creatine phosphokinase in the extracts of liver from cases of both kinds of hepatic cirrhosis: all of these activities were within the range of control values. Similarly, the specific activities of the following lysosomal hydrolases were unremarkable: acid phosphatase, β-mannosidase, β-fucosidase, β-glucuronidase and β-glucosidase. Hexosaminidase specific activity was increased twofold in livers from the cases of cirrhosis due to α(1)-antitrypsin deficiency. The specific activity of a-mannosidase (measured at pH 4.5) in homogenates of livers from P^zz(i) individuals with cirrhosis and those with alcoholic cirrhosis was increased two- to fourfold. Chromatography of the high-speed supernatant fraction from homogenates of livers of cirrhotic and noncirrhotic individuals on columns of DEAE-cellulose resolved a-mannosidase activity into two components: under the conditions employed, acid pH optimum (pH 4.5) α-mannosidase did not bind to the resin, whereas intermediate pH optimum (pH 5.5) α-mannosidase could be eluted with 0.1 mol/1 NaCl. Liver from one case of (Pp) α(1)-antitrypsin deficiency and emphysema, without demonstrable cirrhosis, was found to contain normal levels of both acid α-mannosidase and intermediateα-mannosidase. However, cases of cirrhosis due to α(1)-antitrypsin deficiency contained twice as much acid α-mannosidase and only one third to one fourth as much intermediate amannosidase as controls. The deficiency in hepatic intermediate a-mannosidase was also observed in 5 of 5 cases of alcoholic cirrhosis.

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