Comparison of soluble and membrane-bound neutral arylamidases from renal cell carcinoma.

Soluble and membrane-bound neutral arylamidases from renal cell carcinoma were partially purified and their properties were compared. Soluble neutral arylamidase was a heat labile and SH-dependent metalloenzyme. Membrane-bound neutral arylamidase was a rather heat stable metalloenzyme and was activated by Co2+ with changing KM and VMAX. KM values for soluble and membrane-bound neutral arylamidases were different. L-Methionine (5mM) did not affect the enzymic activity of soluble neutral arylamidase, but inhibited 82 percent of the enzymic activity of membrane-bound neutral arylamidase. Molecular weights of soluble and membrane-bound neutral arylamidases by Sephadex G-200 gel filtration were 140000 and 240000, respectively. Soluble and membrane-bound neutral arylamidases from renal cell carcinoma appear to be distinct enzymes.