Polypeptide synthesis catalyzed by p-hydroxymercuribezoate-modified ribosomes |
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Authors: | Abelardo Lopez-Rivas David Vazquez Enrique Palacian |
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Affiliation: | (1) Instituto de Bioquímica de Macromoléculas, Centro de Biologia Molecular, Consejo Superior de Investigaciones Cientificas and Universidad Autónoma de Madrid, Canto Blanco, Madrid-34, Spain |
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Abstract: | The stimulation of poly(U)-directed polyphenylalanine synthesis produced by modification ofEscherichia coli ribosomes withp-hydroxymercuribenzoate, at low molar ratios of reagent to ribosomes, is due to an increase in the average chain length of polyphenylalanine synthesized, and not to the activation of inactive ribosomes. At a higher molar ratio ofp-hydroxymercuribenzoate to ribosomes, which produces no overall change in activity, approximately 50% of the active ribosomes present in the untreated preparation have been completely inactivated, and the remaining active ones, like the ribosomes of the stimulated preparation, synthesize polyphenylalanine at an increased rate as compared with the untreated ribosomes.Abbreviations pHMB p-hydroxymercuribenzoate - SucNBr N-bromosuccinimide |
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