Abstract
Alkaline RNase was isolated from the pancreas and liver of intact and burned rats and purified 1400 and 2000 times, respectively. The pH-optimum of enzyme activity was 7.6–7.8. Biosynthesis of RNase under normal conditions and after burns was studied by incorporation of labeled amino acids. Inhibition of synthesis of alkaline RNase was found in both organs of the burned animals. The half-life of RNase from the liver of intact rats was 65 min and from the liver of burned animals 100.8 min. Enzymic activity of preparations of alkaline RNase from the liver and pancreas of intact and burned animals did not differ significantly.
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