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

Makoto KIMURA, Catherine K. CHOW

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)225-234
Number of pages10
JournalEuropean Journal of Biochemistry
Volume139
Issue number2
DOIs
Publication statusPublished - Mar 1984

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Geobacillus stearothermophilus
Bacilli
Amino Acid Sequence
Amino Acids
Ribosomal Proteins
Ribosomes
Chromatography
Column chromatography
Proteins
Escherichia coli
ribosomal protein L17
ribosomal proteins L27
ribosomal protein S9

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

The complete amino acid sequences of ribosomal proteins L17, L27, and S9 from Bacillus stearothermophilus. / KIMURA, Makoto; CHOW, Catherine K.

In: European Journal of Biochemistry, Vol. 139, No. 2, 03.1984, p. 225-234.

Research output: Contribution to journalArticle

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