Rutherford K D, Button E E, Kull F J
Comp Biochem Physiol B. 1983;75(3):545-52. doi: 10.1016/0305-0491(83)90373-5.
The effect of an acidic step in the purification of porcine thyroid, latent, alkaline ribonuclease was studied using highly purified acid-treated and non-acid-treated enzymes. The enzymes differed by affinity and CM-cellulose chromatography, specific activity, in distribution among multiple forms, in response to some mono- and divalent salts, in degree of inhibition by p-chloromercuriphenylsulfonate and ribonuclease inhibitor, in activity toward poly (U). The acid-treated enzyme was very heterogeneous as shown by chromatography on affinity and ion-exchange columns and electrophoresis. The enzymes had similar molecular weights, pH optima, ionic strength effects, general specificity and products.