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 | |
| Publication status | Published - Mar 1984 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
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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 journal › Article
}
TY - JOUR
T1 - The complete amino acid sequences of ribosomal proteins L17, L27, and S9 from Bacillus stearothermophilus
AU - KIMURA, Makoto
AU - CHOW, Catherine K.
PY - 1984/3
Y1 - 1984/3
N2 - 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%.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=0021398392&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1984.tb07998.x
DO - 10.1111/j.1432-1033.1984.tb07998.x
M3 - Article
C2 - 6365549
AN - SCOPUS:0021398392
VL - 139
SP - 225
EP - 234
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 2
ER -