RESUMO
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
Interaction of human albumin with immobilized dye-adsorbents was investigated by frontal chromatographic analysis and static adsorption. The relative strength of the interaction is diminished in the following order: cibacron blue F3GA, orange 4K, claret CT, orange 5K, red-brown 2KT, light resistant yellow 2KT, bright blue KX, scarlet 2Zh, bright red 6C, bright yellow 53, red-brown 2K, golden yellow 2KX, scarlet 4ZhT and yellow 2KT. Following this order the absorbents can be used for purification of human albumin from non-specific impurities taking into account stronger adsorption of albumin or impurities. Adsorbents with dyes immobilized on macroporous silica were found to be promising for large-scale purification of human albumin. The silica adsorbent containing red brown 2K is effective for the removal of the following impurities from placental albumin: chorionic gonadotropin, alpha-fetoprotein and placental lactogen.