| Popis: |
Several aminoacyl- t RNA synthetases from the yellow lupin ( Lupinus luteus ) were stabilized against inactivation during storage at 0–4°, by entrapment in Sephadex or Biogel matrices and drying over P 2 O 5 . The degree of stabilization depended on the rate of drying of the gel and the pH of the medium and to a lesser extent on the ionic strength and protein concentration. With the exception of prolyl- t RNA synthetase, a greater stability was achieved with those enzymes which were relatively stable to thermal denaturation. Aminoacyl- t RNA synthetases for glutamic acid, glutamine, methionine and arginine, which become inactivated during purification, were considerably stabilized by this procedure. |
