Abstract
The intensity of incorporation of acetate-1-C14 and glycine-1-C14 into soluble (in 0.14 M NaCl) rat brain and liver proteins under normal conditions and after a stay of 2 h in a pressure chamber at 240 mm Hg was studied. Anoxia inhibited the incorporation of labeled acetate and glycine into the tissue proteins of both organs. Depression of metabolism of soluble liver proteins, unlike that of brain proteins, clearly depends on the degree of lowering of the body temperature.
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