title: [Physico-chemical properties of the thrombolytic compound longolytin].
abstract: A preparation exhibiting high fibrinolytic activity and ability to activate plasminogen was isolated from cultivation medium of Arthrobotrys longa. Homogeneous protein, obtained after gel filtration on Sephadex G-100, had molecular mass 28,600, pI-3.68-3.74, optimum activity at pH 6.0-9.0 and temperature optimum at 37 degrees. The enzyme proved to be serine proteinase as shown by analysis using inhibitors; it required thiol groups.
authors.forename: S A
authors.initials: SA
authors.lastname: Tsymanovich
authors.forename: V N
authors.initials: VN
authors.lastname: Nikandrov
authors.forename: R A
authors.initials: RA
authors.lastname: Maksimova
authors.forename: T S
authors.initials: TS
authors.lastname: Sharkova
authors.forename: G V
authors.initials: GV
authors.lastname: Andreenko
authors.forename: T N
authors.initials: TN
authors.lastname: Serebriakova
mesh_terms: D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D010960:Plasminogen Activators / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D010447:Peptide Hydrolases; C037962:longolytin; D010960:Plasminogen Activators
vernacular_title: Fiziko-khimicheskie svoĭstva tromboliticheskogo preparata longolitina.