Abstract
Isolated non-parenchymal cells from rat liver were separated by centrifugal elutriation into two fractions consisting of structurally intact Kupffer and endothelial cells with purities of 91 and 95%, respectively. Purified Kupffer and endothelial cells showed nearly equal specific activities for the lysosomal enzyme acid phosphatase, whereas the specific activity of cathepsin D was about 3 times higher in Kupffer cells. It was calculated that a significant amount of the cathepsin D activity in the liver is present in the Kupffer cells.
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