Abstract
Rat liver supernatant fractions which are completely free of microsomes and are either freshly prepared or dialysed and freeze-dried, actively incorporate radioactive arginine into their own proteins. The incorporation requires ATP and magnesium ions and is inhibited by iodoacetate, p-chloromercuribenzoate, ribonuclease and, slightly, by deoxyribonuclease. It differs from microsomal protein synthesis in that it is hardly affected by the presence of GTP, of phosphocreatine plus creatine kinase or of a mixture of amino acids, and is relatively insensitive to puromycin or to a change of the KCl in the incubation medium for NaCl. The entire arginine molecule is incorporated in such a way that its α amino group is blocked.
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