title: [Biological properties of L-lysine alpha-oxidase in native and conjugated form].
abstract: The significant difference between biological properties of L-lysine-alpha-oxidase from Trichoderma harzianum Rifai (LO) and L-asparaginase from E. coli has been observed in vitro and in vivo. High antitumor activity was shown against 8 types of murine and rat transplanted tumors with a wide range of LO therapeutic doses: 35-350 U/mg. The LO conjugates with monoclonal antibodies CD5 specific to the surface of cell line Yurkat were obtained without significant loss of either enzymatic and cytotoxic activity or immunological specificity. The further perspective investigation for the clinical application of the native or conjugated enzymes is discussed.
authors.forename: E M
authors.initials: EM
authors.lastname: Treshchalina
authors.forename: O S
authors.initials: OS
authors.lastname: Zhukova
authors.forename: E V
authors.initials: EV
authors.lastname: Lukasheva
authors.forename: L A
authors.initials: LA
authors.lastname: Sedakova
authors.forename: N V
authors.initials: NV
authors.lastname: Andronova
authors.forename: T I
authors.initials: TI
authors.lastname: Solntseva
authors.forename: N V
authors.initials: NV
authors.lastname: Gogichaeva
authors.forename: T T
authors.initials: TT
authors.lastname: Berezov
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D006801:Humans; D019169:Jurkat Cells; D051379:Mice; D051381:Rats
chemical_list: D000911:Antibodies, Monoclonal; D000594:Amino Acid Oxidoreductases; C041123:L-lysine oxidase