Comparison of human membrane-bound neutral arylamidases from small intestine, lung, kidney, liver and placenta.
Human membrane-bound neutral arylamidases were solubilized from small intestinal mucosa, lung, kidney, liver and placenta with trypsin. These five membrane-bound neutral arylamidases were identified by polyacrylamide gel-disc electrophoresis. The heat sensitivity of each enzyme was in the order, liver and placenta greater than kidney greater than lung greater than small intestine. This order correlates with that of electrophoretic mobility, except for the placental membrane-bound neutral arylamidase. Five membrane-bound neutral arylamidases have the same molecular weight, 240 000, as estimated by Sephadex G-200 gel filtration. The five membrane-bound neutral arylamidase have very similar KM values (8.7 x 10(-5) M towards L-alanyl-beta-naphthylamide), optimal pH values, hydrolysis ratios towards L-alanyl-beta-naphthylamide and L-leucyl-beta-naphthylamide, and sensitivities of inhibition by chelators or amino acids. These results suggest that the multiple forms of membrane-bound neutral arylamidase found in five different human organs are organ-specific isoenzymes.
Comparison of human membrane-bound neutral arylamidases from small intestine, lung, kidney, liver and placenta. Human membrane-bound neutral arylamidases were solubilized from small intestinal mucosa, lung, kidney, liver and placenta with trypsin. These five membrane-bound neutral arylamidases were identified by polyacrylamide gel-disc electrophoresis. The heat sensitivity of each enzyme was in the order, liver and placenta greater than kidney greater than lung greater than small intestine. This order correlates with that of electrophoretic mobility, except for the placental membrane-bound neutral arylamidase. Five membrane-bound neutral arylamidases have the same molecular weight, 240 000, as estimated by Sephadex G-200 gel filtration. The five membrane-bound neutral arylamidase have very similar KM values (8.7 x 10(-5) M towards L-alanyl-beta-naphthylamide), optimal pH values, hydrolysis ratios towards L-alanyl-beta-naphthylamide and L-leucyl-beta-naphthylamide, and sensitivities of inhibition by chelators or amino acids. These results suggest that the multiple forms of membrane-bound neutral arylamidase found in five different human organs are organ-specific isoenzymes.