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Ribosomal Proteins, XII. Number of Proteins in Small and Large Ribosomal Subunits of Escherichia coli as Determined by Two-Dimensional Gel Electrophoresis

E. Kaltschmidt, +1 more
- 01 Nov 1970 - 
- Vol. 67, Iss: 3, pp 1276-1282
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TLDR
Two-dimensional gel electrophoresis separates all of the component proteins of the ribosomal subunits of Escherichia coli into 21 and 34 proteins in the 50S, subunit.
Abstract
Two-dimensional gel electrophoresis separates all of the component proteins of the ribosomal subunits of Escherichia coli. This method shows 21 proteins in the 30S, and 34 proteins in the 50S, subunit.

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Journal ArticleDOI

High resolution two-dimensional electrophoresis of proteins.

TL;DR: This technique provides a method for estimation of the number of proteins made by any biological system and can resolve proteins differing in a single charge and consequently can be used in the analysis of in vivo modifications resulting in a change in charge.
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Determination of the number of proteins in liver ribosomes and ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis.

TL;DR: The number of proteins in rat liver ribosome was determined by two-dimensional polyacrylamide gel electrophoresis and it is estimated that eukaryotic ribosomes contain between 68 and 72 different proteins.
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The speciation of the proteome.

TL;DR: To obtain biological relevant information kinetics and systems biology have to be performed at the protein species level, which is the major challenge in proteomics today.
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Ribosomal Proteins in the Spotlight

TL;DR: Although rRNA has a major role in certain aspects of ribosomal function, such as decoding and peptidyl-transferase activity, ribosomic proteins are nevertheless essential for the assembly and optimal functioning of the ribosome.
Journal ArticleDOI

The Primary Structure of an Acidic Protein from 50-S Ribosomes of Escherichia coli which is Involved in GTP Hydrolysis Dependent on Elongation Factors G and T

TL;DR: The distinctive clustering of hydrophobic and charged residues is quite remarkable and suggests that in situ certain of these regions may contain a binding site for components involved in peptide chain elongation.
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