The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus
- 30 January 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 166 (2), 343-346
- https://doi.org/10.1016/0014-5793(84)80109-x
Abstract
The low-M r proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205–214]. Protein I contains 56 residues and has an M r of 6514. Protein II had 37 residues with an M r of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.Keywords
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