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Abstract
Activity of α-amylase and α-1,4-glucosidase was studied in subfractions of human liver homogenates obtained from operative biopsies in 22 patients operated on for uncomplicated gallstone disease. No activity of α-amylase was found in subfractions of homogenate. The activity of α-1,4-glucosidase was distributed in the same way as acid phosphatase and β-glucuronidase activity upon centrifugal fractionation of homogenate. The highest activity of α-1,4-glucosidase per unit of protein was found in the crude lysosomal fraction (L-fraction). The activity was easily solubilized from the L-fraction pellet. The lysosomal origin of the enzyme appears unambiguous considering its subcellular distribution and its acid hydrolytic properties.