Characterization and comparison of ribosomal proteins from two prokaryotic organisms

Richard Gregory, Isaac L. Shechmeister

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Ribosomal proteins from the prokaryotic bacteria. Streptococcus mutans and Escherichia coli, were separated by two dimensional gel electrophoresis as described by O'Farrell. The resulting protein spot patterns in the two types of gels are discussed in comparison with one another and with ribosomal proteins from eukaryotic organisms. More acidic proteins were found in ribosomal preparations from E. coli than from S. mutans, although this was probably a result of contamination of the former preparation with cellular components. Six ribosomal proteins from these organisms traversed to similar positions on the gels and this suggested that they were identical with respect to molecular weight and electrostatic charge. The data indicate that the six proteins were conserved through the evolution of these two prokaryotic organisms.

Original languageEnglish (US)
Pages (from-to)113-116
Number of pages4
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume76
Issue number1
DOIs
StatePublished - 1983
Externally publishedYes

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Ribosomal Proteins
Streptococcus mutans
Gels
Escherichia coli
Proteins
Electrophoresis, Gel, Two-Dimensional
Electrophoresis
Static Electricity
Electrostatics
Bacteria
Contamination
Molecular Weight
Molecular weight

Cite this

Characterization and comparison of ribosomal proteins from two prokaryotic organisms. / Gregory, Richard; Shechmeister, Isaac L.

In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 76, No. 1, 1983, p. 113-116.

Research output: Contribution to journalArticle

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