[The effect of pH value and temperature on the stability of L-aminoacidoxidase from the venom of the sand viper].
The stability of highly purified L-amino acid oxidase from the sand viper venom remains practically unaffected by the pH-value at 4degreesC between pH 5 and 8, whereas a sharp activity fall was observed on both sides of this range. At temperatures above 30 degreesC the enzyme is stable only at pH 5.0--5.5. The inactivation pH values above 5.5 follows a first-order rate equation with characteristic changes in the absorption and emission spectra of the enzyme. The stability of the enzyme is dependent on the temperature of storage. At pH 7.5 there is a stability minimum at --10 degrees and -- 30 degreesC. At -- 72 degreesC the enzyme is stable practically for an unlimited period of time; temperatures exceeding 50 degrees C rapidly lead to complete inactivation. Also in the cold, the L-amino acid oxidase is most stable at pH 5.5. There are characteristic changes in absorption and emission spectra in the temperature-stability minimum (--15 degreesC) and at temperatures above 30degreesC. The inactivations follow a first-order rate equation. The cold inactivation is reversible. The stability of the enzyme is diminished by some anions and cations at 37 degreesC. The cold inactivation is promoted by several inorganic anions; organic anions and ammonium sulfate prevent cold inactivation.
D000594:Amino Acid Oxidoreductases; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D012910:Snake Venoms / Q000032:analysis; D013696:Temperature
D012910:Snake Venoms; D000594:Amino Acid Oxidoreductases
Einfluss von pH-Wert und Temperatur auf die Stabilität der L-Aminosäureoxydase aus dem Gift der Sandotter