Some properties of lysosomal arylamidase in rat liver.
Lysosomal arylamidase in rat liver was reassessed. The arylamidase was distinguishable into seven types having different isoelectric points by isoelectric fractionation. All the types hydrolyzed valine beta-naphthylamide most rapidly among amino acid beta-naphthylamides tested, but did not hydrolyze arginine beta-naphthylamide. These enzymes exhibited maximum activities at pH 7.0. They had a molecular weight of 135,000 by gel filtration on a Sephacryl S-200. They were all inhibited by sulfhydryl-blocking reagents and activated by sulfhydryl compounds, indicating to be cysteine proteases.
Hiroi
Y
Y
Department of Nutritional Chemistry, Nakamura Gakuen College, Fukuoka, Japan.
Toku
S
S
D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000378:metabolism; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007526:Isoelectric Point; D007527:Isoenzymes; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D009281:Naphthalenes / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D014633:Valine / Q000378:metabolism
D007527:Isoenzymes; D009281:Naphthalenes; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; C072587:2-naphthylamide; D001120:Arginine; D000626:Aminopeptidases; D003546:Cysteine Endopeptidases; D014633:Valine