title: [Cytolytic activity of Legionella pneumophila].
abstract: The properties of cytolysin and metalloproteinase purified by different methods have been studied. The physico-chemical properties of these proteins, including their molecular weight, immunodiffusion patterns, the degree of inhibition by EDTA and diethyl pyrocarbonate, amino acid composition, cytolytic and proteolytic activity, have proved to be similar. We have come to the conclusion that cytolysin and metalloproteinase have similar composition and metalloproteinase activity determines the cytolytic and necrotic activity of the above-mentioned cytolysin.
authors.forename: Iu F
authors.initials: IuF
authors.lastname: Belyĭ
authors.forename: I S
authors.initials: IS
authors.lastname: Tartakovskiĭ
authors.forename: S V
authors.initials: SV
authors.lastname: Gul'nik
authors.forename: G I
authors.initials: GI
authors.lastname: Lavreneva
authors.forename: V M
authors.initials: VM
authors.lastname: Stepanov
mesh_terms: D000596:Amino Acids / Q000032:analysis; D003603:Cytotoxins / Q000302:isolation & purification*; D006868:Hydrolysis; D005779:Immunodiffusion; D007875:Legionella / Q000201:enzymology / Q000378:metabolism* / Q000472:pathogenicity; D008666:Metalloendopeptidases / Q000378:metabolism*; D008970:Molecular Weight
chemical_list: D000596:Amino Acids; D003603:Cytotoxins; D008666:Metalloendopeptidases
vernacular_title: Priroda tsitoliticheskoĭ aktivnosti Legionella pneumophila.