## Abstract Artificial amino acids carrying either the chromophore of the Green Fluorescent Protein (GFP) or a modification as their side chains have been synthesized: Boc‐protected alaninyl derivatives and Fmoc‐protected __N__‐(2‐aminoethyl)glycine‐functionalized amino acids were obtained and coul
Energy requirement for the incorporation of amino acids into protein of isolated mouse-liver mitochondria
✍ Scribed by Patrick F. Delaney; Norman J. Girardot
- Publisher
- John Wiley and Sons
- Year
- 1966
- Tongue
- English
- Weight
- 238 KB
- Volume
- 68
- Category
- Article
- ISSN
- 0021-9541
No coin nor oath required. For personal study only.
✦ Synopsis
Mitochondria isolated from mouse liver can incorporate amino acids into mitochondrial protein. Studies with oligomycin and antihistamine drugs indicate that this incorporation may not be an ATP requiring process.
Several laboratories '55; Truman and Korner, '62; Bronk, '63; Kalf, '63) have reported that isolated mitochondria incorporate amino acids into mitochondrial protein without the addition of supernatant fractions. Truman and Korner ('62) and Bronk ('63) have demonstrated that oxidizable substrate provided a better energy source for this process than added adenosine triphosphate (ATP).
Bronk ('63) found that 0.3 vg/ml of oligomycin did not inhibit mitochondrial incorporation of amino acid into protein, even though this concentration of oligomycin blocked the terminal phosphorylation steps of ATP formation. Bronk also
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## Abstract **The cover picture shows** a chromophore of the Green Fluorescent Protein, which undergoes fast internal conversion by rotation causing the quenching of its fluorescence in solution. In contrast, the intact protein shows a high fluorescence quantum yield and there is still a need to un