title: A novel thermophilic lysozyme from bacteriophage phiIN93.
abstract: The lysozyme of bacteriophage phiIN93 was purified to apparent homogeneity with Carboxymethyl Sepharose and Hydroxyapatie columns from lysates of the phage grown on Thermus aquaticus TZ2. The enzyme is a single polypeptide chain with a molecular weight of 33,000. From the determined N-terminal amio acids of the enzyme, the locus of the gene was specified on a phiIN93 genome. The enzyme was not similar to egg white lysozyme, T4 phage lysozyme, or lambda phage lysozyme. The enzyme, phiIN93 lysozyme, was found to be a novel type of thermophilic lysozyme, which lyses specifically Thermus sp. cells, and exhibited conspicuous thermal stability at 95 degrees C for 1h in the presence of beta-mercaptoethanol.
authors.affiliation: Energy Technology Laboratories, Osaka gas Co, Ltd, Torishima, Osaka, Japan. imatsu@osakagas.co.jp
authors.forename: Isao
authors.initials: I
authors.lastname: Matsushita
authors.forename: Hideshi
authors.initials: H
authors.lastname: Yanase
mesh_terms: D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000201:enzymology* / Q000235:genetics; D005814:Genes, Viral; D006358:Hot Temperature; D008623:Mercaptoethanol / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D013379:Substrate Specificity; D013824:Thermus / Q000821:virology*; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D014764:Viral Proteins; D008623:Mercaptoethanol; D009113:Muramidase