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  • Title: Subcellular distribution of soluble and membrane-bound Leu-, Arg- and Asp-beta-naphthylamide-hydrolysing activities in rat brain.
    Author: Ramirez M, Arechaga G, Lardelli P, Venzon D, de Gandarias JM.
    Journal: Cell Mol Biol; 1990; 36(2):175-9. PubMed ID: 2379231.
    Abstract:
    Subcellular distribution of soluble and membrane-bound Leu-, Arg- and Asp-beta-naphthylamide hydrolysing activities (arylamidase activity) was studied from left and right rat brains, each including hemisphere, cerebellum and brain stem. Both soluble Leu- and Arg-beta-naphthylamide hydrolysing activities showed the highest levels in the synaptosomal fraction. However, the microsomal fraction presented the highest levels when membrane-bound activity was assayed. When we used Asp-beta-naphthylamide as substrate, there were no differences among fractions in the membrane-bound activity, and the highest soluble activity was present at the mitochondrial level. Two different patterns in the subcellular distribution of enzymatic activity were observed: One of them was the result of the use of Leu- or Arg-beta-naphthylamide as substrate and the other when Asp-beta-naphthylamide was employed. No differences between left and right brains in soluble or membrane-bound activities were found.
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