Action Philosophers! 01 - Nietzsche, Bodhidharma, & Plato: by Evil Twin Comics

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Extra info for Action Philosophers! 01 - Nietzsche, Bodhidharma, & Plato: ''Wrestling Superstar of Ancient Greece!'' - Apr2005

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1973). , 1971), that for binding of monoiodoamphenicol is one order of magnitude higher. Many antibiotics which also bind to the 50 S subunit inhibit in turn, binding chloramphenicol to ribosomes (review : VAZQUEZ, 1975). These antibiotics include macrolides (angolamycin, carbomycin, erythromycin, lancamycin, spiramycin), 4-aminohexose pyrimidine nucleosides (amicetin, blasticidin S, gougerotin), lincomycin, puromycin, sparsomycin, streptogramin A, and streptogramin B. Carbomycin is a strong inhibitor of chloramphenicol binding.

These antibiotics include macrolides (angolamycin, carbomycin, erythromycin, lancamycin, spiramycin), 4-aminohexose pyrimidine nucleosides (amicetin, blasticidin S, gougerotin), lincomycin, puromycin, sparsomycin, streptogramin A, and streptogramin B. Carbomycin is a strong inhibitor of chloramphenicol binding. , 1966). The 4-aminohexose pyrimidine nucleosides do not inhibit chlorampheni- Chloramphenicol 33 col binding as strongly as the macrolides. , 1971; LESSARD and PESTKA, 1972). Therefore, it was proposed that the chloramphenicol receptor site is part of that site of the ribosomal peptidyl transferase center (A-site) where the 3'terminus of aminoacyl-tRNA becomes bound (review: PONGS, 1977).

Bacteriol. : Specific biosynthesis of an envelope protein of Escherichia coli. : Differential inhibitory effects of antibiotics on the biosynthesis of envelope proteins of Escherichia coli. J. Mol. BioI. : Two forms of a structural lipoprotein in the envelope of Escherichia coli. Further characterization of the free form. J. BioI. Chern. : Cell-free synthesis of a specific lipoprotein of the Escherichia coli outer membrane directed by purified messenger RNA. Proc. Nat!. Acad. Sci. : On the process of cellular division in Escherichia coli: A mutant of E.

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