Authors : M. BELJANSKI, S. OCHOA
Department of Biochemistry, New York University College of Medicine, NY
IV-ème Congrès Intern. Biochim. Vienne, 1958, p.49 – Résumés des commnunications.
Available in French only
ABSTRACT: Indications have been obtained for the presence ot the amino acid incorporation enzyme in the supernatant fraction from rat liver and in the precipitate obtained by acidification of this fraction to pH 5.2 (pH 5 enzymes). Highly purified amino acid incorporation enzyme from A. faecalis completely replaces the pH 5 enzymes in stimulating the incorporation of C14-leucine into protein of rat livermicrosomes. These observations show that the amino acid incorporation enzyme is involved in protein biosyntheses of both mammalian and bacterial cells.
Highly purified preparations of the A. faecalis incorporation enzyme catalyze a rapid, Mg++dependent exchange a radioactive ADP with ATP an activity which appears to be related to their amino acid incorporation activity. This finding may be of significance, since glutathione synthetase, which catalyzes the synthesis of a typical peptide, brings about a similar exchange.