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PMID: 371684 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

A purified nucleoprotein fragment of the 30 S ribosomal subunit of Escherichia coli.

Biochimica et biophysica acta ·Vol. 561 ·No. 2 ·1979-02-27 ·Pages 435-44

Spitnik-Elson P, Elson D, Abramowitz R

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 . 10(5) and 2.5 . 10(4) 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.

MeSH Terms
Escherichia coli/analysis Molecular Weight Nucleoproteins/isolation & purification RNA, Ribosomal/isolation & purification Ribonucleoproteins/isolation & purification Ribosomal Proteins/isolation & purification Ribosomes/analysis
Chemicals
Nucleoproteins RNA, Ribosomal Ribonucleoproteins Ribosomal Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Spitnik-Elson P
Elson D
Abramowitz R
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1979-02-27
Pages
435-44
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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