The activities of ß-N-acetylglucosaminidase, β-glucuronidase, α-L-iduronidase
and acid phosphatase were all significantly higher in the cell lysates from the periportal than
from the perivenous region obtained by the regioselective digitonin treatment of the perfused
liver. The activities of cathepsins B, H and L were only slightly higher in the periportal than
in the perivenous cell lysates. These results support the view that there is little zonation of
lysosomal degradation of proteins, whereas the enzymatic capacity for degradation of glycosaminoglycans
may be more active in the periportal region.
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