A purified nucleoprotein fragment of the 30 S ribosomal subunit of Escherichia coli |
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Affiliation: | 1. Department of Biological Sciences, Wayne State University, Detroit, MI, 48202, USA;2. Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, 15260, USA;1. Lomonosov Moscow State University, Faculty of Biology, Moscow, 119234, Russia;2. Federal Research Center “Fundamentals of Biotechnology” RAS, Moscow, 119071, Russia;3. Semenov Federal Research Center of Chemical Physics, RAS, Moscow, 119991, Russia;4. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, RAS, Moscow, 117997, Russia |
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Abstract: | A ‘13 S’ nucleoprotein fragment was isolated from a nuclease digest of Escherichia coli 30-S ribosomal subunits and purified to gel electrophoretic homogeneity. It contained two polynucleotides, of about 1.1 · 105 and 2.5 · 104 daltons, which separated when the fragment was deproteinized. The major protein components were S4, S7 and S9/11, with S15, S16, S18, S19 and S20 present in reduced amount. |
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