title: Purification and characterization of new arginine esteropeptidase from the soluble fraction of human submaxillary glands.
abstract: An arginine esteropeptidase was completely purified from the soluble fraction of human submaxillary glands. The molecular weight was calculated to be 12,000, having 2 species of subunits. The study of the effect of inhibitors confirmed the enzyme's serine protease-like characteristics. The best ester and amide substrates were Tos-Arg-OMe and D-Ile-Pro-Arg-pNA, respectively.
authors: Hokkaido Institute of Pharmaceutical Sciences, Japan.
authors: Y
authors: Y
authors: Fujimoto
authors: M
authors: M
authors: Suzuki
authors: Y
authors: Y
authors: Watanabe
mesh_terms: D000595:Amino Acid Sequence; D002847:Chromatography, Agarose; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D012995:Solubility; D013363:Submandibular Gland / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D009842:Oligopeptides; D001121:Lysine Carboxypeptidase