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.
D000230:Adenocarcinoma / Q000201:enzymology*; D000626:Aminopeptidases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D003035:Cobalt / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007680:Kidney Neoplasms / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D010618:Phenanthrolines / Q000494:pharmacology
D010618:Phenanthrolines; D003035:Cobalt; D000626:Aminopeptidases