Purification and characterization of new arginine esteropeptidase from the soluble fraction of human submaxillary glands.
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.
Fujimoto
Y
Y
Hokkaido Institute of Pharmaceutical Sciences, Japan.
Suzuki
M
M
Watanabe
Y
Y
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
D009842:Oligopeptides; D001121:Lysine Carboxypeptidase