Arginine Esterase and Lysosomal Hydrolases in Liver from Cystic Fibrosis Subjects

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Abstract
Summary: The total activity and isoelectric focusing patterns of arginine esterase, cathepsin B1, and several lysosomal hydrolases were normal in liver from two patients with cystic fibrosis. No abnormalities were observed in values for pH optimum, Km, and Vmax for arginine esterase and cathepsin B1 in liver from cystic fibrosis patients compared to those values for liver from the control subject. Soybean trypsin inhibitor at concentrations up to 100 μg/ml had no effect on liver arginine esterase or cathepsin B1. Speculation: The data suggest that none of the enzymes studied in this work is directly related to the genetic defect in cystic fibrosis. Liver arginine esterase is different from the major arginine esterase found in plasma and saliva but may be identical to the minor component. The reported deficiency (12–15) of the major plasma arginine esterase may be a secondary phenomenon resulting from inadequate exocrine (chiefly pancreatic) secretion.

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