The complete amino acid sequences of ribosomal proteins L17, L27, and S9 from Bacillus stearothermophilus

Makoto KIMURA; Catherine K. CHOW

doi:10.1111/j.1432-1033.1984.tb07998.x

The complete amino acid sequences of ribosomal proteins L17, L27, and S9 from Bacillus stearothermophilus

Makoto KIMURA, Catherine K. CHOW

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

The complete primary structures of proteins L17, L27 and S9 extracted from the Bacillus stearothermophilus ribosomes with 1 M NaCl and purified to homogeneity by column chromatography have been determined. The amino acid sequences of these proteins are compared to those of the homologous ribosomal proteins from Escherichia coli. The number of identical amino acid residues between the homologous proteins lies between 33–55%.

Original language	English
Pages (from-to)	225-234
Number of pages	10
Journal	European Journal of Biochemistry
Volume	139
Issue number	2
DOIs	https://doi.org/10.1111/j.1432-1033.1984.tb07998.x
Publication status	Published - Mar 1984

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1111/j.1432-1033.1984.tb07998.x

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abstract = "The complete primary structures of proteins L17, L27 and S9 extracted from the Bacillus stearothermophilus ribosomes with 1 M NaCl and purified to homogeneity by column chromatography have been determined. The amino acid sequences of these proteins are compared to those of the homologous ribosomal proteins from Escherichia coli. The number of identical amino acid residues between the homologous proteins lies between 33–55%.",

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