Mechanism of incorporation of labeled amino acids into protein

✍ Scribed by Zamecnik, P. C. ;Keller, E. B. ;Littlefield, J. W. ;Hoagland, M. B. ;Loftfield, R. B.

• Publisher: Wiley (John Wiley & Sons)
• Year: 1956
• Tongue: English
• Weight: 1018 KB
• Volume: 47
• Category: Article
• ISSN: 0095-9898
• DOI: 10.1002/jcp.1030470408

✦ Synopsis

FIVE FIGURES

I n this supplement, a general review of studies on the mechanism of protein synthesis is presented by H. Borsook.

The present discussion may therefore, with less embarrassment, be confined to a presentation of recent experimental findings from a single laboratory. These results are concerned principally with cell-free preparations from rat livers, and will be introduced under four main headings.

I n 1941 Lipmann prophesied that phosphate-bond energy drove the process of protein synthesis. The availability of Cx4 in the postwar years made it possible t o devise an experimental test of this suggestion. Using dinitrophenol (DNP), Frantz et al. ('48) found a parallelism between the inhibition of phosphorylation and of amino acid incorporation, in liver slices. Siekevitz ( '52 ; Siekevitz and Zamecnik, '51) extended this theme to a cell-free system, demonstrating a relation between oxidative phosphorylation and amino acid incorporation in a crude rat liver homogenate. Other evidence for the participation of phosphate-bond energy in the synthesis of protein and of peptidic bonds had also continued to accumulate (Speck, '47; Elliott, '48; Bloch, '49; Peterson and Green-* Supported by grants-in-aid from the U. s.