Membrane-bound arylamidase from human hepatoma cells having the same electrophoretic mobility as placental membrane-bound arylamidase.
A membrane-bound arylamidase from well-differentiated hepatocellular carcinoma having the same electrophoretic mobility as placental membrane-bound arylamidase was found. The enzyme was found to be a sialoprotein and was activated by Co2+. Hepatoma membrane-bound arylamidase had a similar molecular weight (240 000) and kinetic properties to normal liver membrane-bound arylamidase, but differed from the liver enzyme with respect to electrophoretic mobility, heat stability and urea inactivation.
D000626:Aminopeptidases / Q000302:isolation & purification*; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D003035:Cobalt; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D008113:Liver Neoplasms / Q000201:enzymology*; D008970:Molecular Weight; D009439:Neuraminidase; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D012795:Sialoglycoproteins
D012795:Sialoglycoproteins; D003035:Cobalt; D009439:Neuraminidase; D000626:Aminopeptidases