[Catalytic properties of induced L-lysine-alpha-oxidase]. / Izuchenie kataliticheskikh svoistv indutsirovannoi L-lizin-alpha- oksidazy.

Regulation of biosynthesis of L-lysine-alpha-oxidase from Trichoderma sp using biostimulators was studied. Specific activity of L-lysine-alpha-oxidase was increased 2.7-fold in presence of biostimulators; this occurred due to induction of the enzyme, properties of which were described previously. Catalytic and physico-chemical properties of the enzyme studied were not altered after addition of stimulators into the cultivation medium of the producing strain. Small amounts of L-lysine-alpha-oxidase isozyme were detected in the medium during cultivation; the isozyme was less active and had lower molecular mass as compared with the enzyme studied.

[A new method of purification of L-lysine-alpha-oxidase from the fungus Trichoderma]. / Novyi metod ochistki L-lizin-alpha-oksidazy griba Trichoderma.

A new procedure is developed for purification of the antitumoral enzyme L-lysyl-alpha-oxidase from Trichoderma sp. The procedure included two steps: hydrophobic chromatography on butyl sylochrome C-80 and chromatography using biospecific sorbent AH-Sepharose. The simplified procedure enabled to increase distinctly the specific enzymatic activity from 30 to 50 IU/mg in the preparation obtained with a good yield.

[Evaluation of antileukemic activity of L-lysine-alpha oxidase from Trichoderma sp. in chemotherapeutic experiments]. / Otsenka protivoleikoznoi aktivnosti L-lizin-alfa-oksidaza iz Trichoderma sp. v khimioterapevticheskikh opytakh.

Evidences on the antileukemic effect of L-lysine alpha-oxidase from Trichoderma sp. are presented. It is inferred that enzyme needs detail studying as a potential chemotherapeutic drug both in experimental and clinical research.

[Improved method of purification of L-lysine-alpha-oxidase from the fungus Trichoderma sp]. / Usovershenstvovannaia skhema ochistki L-lizin-alpha-oksidazy griba Trichoderma sp.

Relatively rapid procedure was developed for isolation and purification of the antitumor enzyme L-lysine alpha-oxidase. The procedure involved three steps instead of six or four steps described previously, with a yield of 64.4%. The homogenous preparation was obtained as shown by gel electrophoresis and ultracentrifugation. The antitumor activity of the enzyme both in vivo and in vitro is under investigation.

[Various physico-chemical properties of L-lysine-alpha-oxidase from Trichoderma sp]. / Nekotorye fiziko-khimicheskie svoistva L-lizin-alpha-oksidazy iz Trichoderma sp.

L-lysine-alpha-oxidase, isolated from a strain of Trichoderma sp. exhibited enzymological properties suitable for a chemotherapeutic drug used in experimental oncology.