title: Effective method for purification of lysozyme from human urine.
abstract: Lysozyme in the urine of a hemodialysis patient was purified in two steps: DEAE Sephadex chromatography followed by Sephacryl chromatography. The Sephacryl S-100 column chromatographed fraction showing lytic activity was proven to give one band on SDS-PAGE and to have a molecular mass of 14500, in agreement with that of lysozyme. The N-terminal amino acid sequence of this purified protein was identical to that of lysozyme. These results indicate that the protein purified was indeed lysozyme. The specific affinity of lysozyme for Sephacryl S-100 may explain the greater purity of the same protein isolated by this method.
authors.affiliation: Department of Internal Medicine, Branch Hospital, Nagoya University School of Medicine, Japan.
authors.forename: I
authors.initials: I
authors.lastname: Takai
authors.forename: O
authors.initials: O
authors.lastname: Oda
authors.forename: T
authors.initials: T
authors.lastname: Shinzato
authors.forename: K
authors.initials: K
authors.lastname: Ohbayashi
authors.forename: N
authors.initials: N
authors.lastname: Yamanaka
authors.forename: K
authors.initials: K
authors.lastname: Maeda
mesh_terms: D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D009113:Muramidase / Q000652:urine*
chemical_list: D009113:Muramidase