[Preparation and study of properties of immobilized phosphodiesterases from blunt-nosed viper venom].
From gurza poison phosphodiesterase covalently bound with DEAE-cellulose via triazine dye was isolated. Immobilized phosphodiesterase retained 100% activity of the initial enzyme. The effect of pH, temperature. Mg++ concentration on the immobilized enzyme activity was studied. Preparations of the immobilized enzyme did not lose their activity upon hydrolysis of oligodeoxy- and ribonucleotides during a month and remained suitable for prolonged hydrolysis of preparative quantities of oligonucleotides.
D002848:Chromatography, DEAE-Cellulose; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008274:Magnesium; D009838:Oligodeoxyribonucleotides / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D012265:Ribonucleotides / Q000378:metabolism; D013696:Temperature; D014757:Viper Venoms / Q000201:enzymology*
D004800:Enzymes, Immobilized; D009838:Oligodeoxyribonucleotides; D012265:Ribonucleotides; D014757:Viper Venoms; D010727:Phosphoric Diester Hydrolases; D008274:Magnesium
Poluchenie i issledovanie svoĭstv immobilizovannoĭ fosfodiésterazy iz iada giurzy.