Abstract
IN Zamecnik's laboratory, Frantz et al. 1 using dinitrophenol, found in liver slices a parallelism between the inhibition of phosphorylation and of amino-acid incorporation. Siekevitz2 demonstrated in a cell-free system a relation between oxidative phosphorylation and amino-acid incorporation in a crude rat-liver homogenate. Hoagland3 concluded from his experiments that the carboxyl groups of the amino-acids are activated by adenosine triphosphate, and that the activated amino-acyl groups are bound through an adenosine monophosphate bridge to an enzyme acting as an intermediate amino-acyl transfer compound. However, such intermediates have not yet been isolatedand identified. In their systems it was not possible to ‘exchange out’ the carbon-14 labelled amino-acids with large quantities of unlabelled amino-acids ; thus the incorporation was different from the exchange process described by Gale and Folkes4 in fragmented Staphylococcus aureus. J. T. Park5 has isolated uridine-5′-phosphate derivatives containing an amino-sugar and amino-acids from extracts of Staphylococcus aureus treated with penicillin. On the basis of these and a great number of other experiments, Borsook6 proposed a hypothesis for the mechanism of biosynthesis : the carboxyl groups of free amino-acids are first activated by an enzyme system dependent on adenosine triphosphate. They are then transported to a nucleic acid template by an unknown mechanism and are arranged in a specific sequence, the amino-acids being attached to the phosphate of nucleic acid by their carboxyl groups. On this template, the amino-acids are then linked by peptide bonds through the action of another enzyme, and the protein molecule peels off the template.
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References
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REITH, W. Incorporation of Radioactive Aspartic Acid into the Proteins and Related Fractions in Mice bearing the Ehrlich Ascites Carcinoma. Nature 178, 1393–1394 (1956). https://doi.org/10.1038/1781393a0
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DOI: https://doi.org/10.1038/1781393a0