RESUMO
L-lysine-alpha-oxidase, isolated from a strain of Trichoderma sp. exhibited enzymological properties suitable for a chemotherapeutic drug used in experimental oncology.
Assuntos
Aminoácido Oxirredutases/isolamento & purificação , Antineoplásicos , Fungos Mitospóricos/enzimologia , Trichoderma/enzimologia , Aminoácido Oxirredutases/farmacologia , Antineoplásicos/isolamento & purificação , Cromatografia em Gel , Concentração de Íons de Hidrogênio , Focalização Isoelétrica , Cinética , Peso Molecular , Especificidade da Espécie , Especificidade por SubstratoRESUMO
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.
Assuntos
Aminoácido Oxirredutases/isolamento & purificação , Fungos Mitospóricos/enzimologia , Trichoderma/enzimologia , Cromatografia DEAE-Celulose , L-Aminoácido Oxidase , Especificidade por SubstratoRESUMO
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.
Assuntos
Aminoácido Oxirredutases/biossíntese , Catálise , Eletroforese em Gel de Poliacrilamida , Indução Enzimática , Estabilidade Enzimática , Concentração de Íons de Hidrogênio , Especificidade por Substrato , Trichoderma/enzimologiaRESUMO
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.
Assuntos
Aminoácido Oxirredutases/isolamento & purificação , Trichoderma/enzimologia , Cromatografia/métodosRESUMO
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.