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Erythromycin, lincosamides, peptidyl-tRNA dissociation, and ribosome editing (1994)

Menninger, John R. ; Coleman, Ruth A. ; Tsai, Lee-Na

Springer

Molecular genetics and genomics 243 (1994), S. 225-233

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ISSN: 1617-4623

Keywords: Protein synthesis ; Translation ; Accuracy ; Macrolide antibiotics

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Inaccurate protein synthesis produces unstable β-galactosidase, whose activity is rapidly lost at high temperature. Erythromycin, lincomycin, clindamycin, and celesticetin were shown to counteract the error-inducing effects of streptomycin on β-galactosidase synthesized in the antibiotic-hypersensitive Escherichia coli strain DB-11 Met −. Newly synthesized β-galactosidase was more easily inactivated by high temperatures when synthesized by bacteria partially starved for arginine, threonine, or methionine. Simultaneous treatment with erythromycin or linocomycin yielded β-galactosidase that was inactivated by high temperatures less easily than during starvation alone, an effect attributed to stimulation of ribosome editing. When synthesized in the presence of canavanine, β-galactosidase was inactivated by high temperature more easily but this effect could not be reversed by erythromycin. The first arginine in β-galactosidase occurs at residue 13, so the effect of erythromycin during arginine starvation is probably to stimulate dissociation of erroneous peptidyl-tRNAs of at least that length. Correction of errors induced by methionine starvation is probably due to stimulation of dissociation of erroneous peptidyl-tRNAs bearing peptides at least 92 residues in length. All the effects of erythromycin or the tested lincosamides on protein synthesis are probably the result of stimulating the dissociation from ribosomes of peptidyl-tRNAs that are erroneous or short.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00280320

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Graft copolymer of gelatin/butyl acrylate and its use in the dye transferring blank film (1989)

Li, Zhi-Chong ; Fu, Zhi-Feng ; Huang, Ming-Zhi ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Applied Polymer Science 38 (1989), S. 2171-2182

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ISSN: 0021-8995

Keywords: Chemistry ; Polymer and Materials Science

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics

Notes: Butyl acrylate was graft copolymerized onto gelatin using ceric ammonium nitrate as redox initiator. A series of grafted products with various gelatin-to-butyl acrylate ratios were prepared. The molecular weight of the grafted side chains and the number of grafting sites were measured. The possible grafting sites on gelatin macromolecules were pointed out through amino acid analysis. The electron micrograph and DSC analysis showed that the grafted chain (PBA) and backbone gelatin were in separated phases. The graft copolymer was used in the receiving layer of the dye transfer blank film, and the photographic, dye transfer printing, and some physicomechanical properties were studied with satisfactory results.

Additional Material: 4 Ill.