By Wilbur A. Smith

The number 1 overseas Bestseller

Game of Thrones meets historical Egypt during this very good epic from one of many world's biggest-selling authors. Conjuring the magic, secret and bloody intrigue of a desirable misplaced international, Desert God provides Wilbur Smith on the helm of 1 of the best tales of all time.

On the sparkling banks of the Nile, the bright Taita—a freed slave and consultant to the Pharaoh—devises a plan to break Egypt's so much feared enemy, the strong Hyksos. His quest will take him on an epic trip up the traditional river, via Arabia and the paranormal urban of Babylon and around the open seas—all within the corporation of the Pharaoh's beautiful sisters. With the way forward for the dominion itself on his shoulders, Taita plunges right into a international the place the road among loyalty and betrayal shifts just like the barren region sands, evil waits within the shadows and demise lingers at the fringe of darkness.

Hundreds of thousands have fallen in love with the magic of Wilbur Smith. In Desert God, he's on the top of his powers, transporting readers to a rare time and position. this can be a novel of ideal experience, blazing motion, heart-racing romance and a feeling of historical past so genuine that you're going to think the dunes relocating underneath you and the Nile lapping at your ft.

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Additional resources for Desert God (Ancient Egypt, Book 5)

Sample text

34 O. PONGS On the other hand, some studies on the effects of chloramphenicol on peptide bond formation suggest that it does not bind to the peptidyl acceptor site of the ribosome, but to the peptidyl donor site (for a thorough discussion of these data, see HAHN and GUND, 1975). The point of view relies heavily on observations that chloramphenicol inhibits peptide bond formation much more strongly when the peptidyl donor site is occupied by peptidyl residues rather than ~ artificially ~ by aminoacyl-tRNA.

J. BioI. Chern. : Chloramphenicol inhibition of polyuridylic acid binding to E. coli ribosomes. : Chloramphenicol. In: Khimia Antibiotikow I. : Drug Resistance of Staphylococci. XI. Induction of chloramphenicol resistance by its derivatives and analogues. Japan. J. Microbiol. : Protein Synthesis in heart mitochondria. I. Amino acid incorporation into the protein of isolated beef-heart mitochondria and fractions derived from them by sonic oscillation. Biochim. Biophys. , Lipmann, F. : Differences in chloramphenicol sensitivity of cell-free amino acid polymerization systems.

Mol. BioI. : Identification of chloramphenicol-binding protein in Escherichia coli ribosomes by affinity labeling. Proc. Natl. Acad. Sci. : Active sites in Escherichia coli ribosomes. FEBS-Lett. Suppl. : In "Topics in Infectious Diseases. Drug Receptor Interactions in Antimicrobial Chemotherapy" (J. Drews a. E. ). Vol. 1, 179-190. : Chloramphenicol (chloromycetin). J. Am. Chern. Soc. : Some compounds related to chloromycetin. J. Chem. Soc. 77, 24-26 (1955) Rendi, R. : The effect of chloramphenicol on the incorporation of labeled amino acids into proteins by isolated subcellular fractions from rat liver.

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