| Literature DB >> 1100506 |
K G Bitar, B Wittmann-Liebold.
Abstract
The primary structure of protein L25 from the large subunit of Escherichia coli ribosomes was determined by isolation and analysis of peptides obtained after cleavage of the protein with trypsin, thermolysin and Staphylococcus protease as well as by Edman degradation of the intact protein and of a CNBr peptide. The complete amino acid sequence is shown in Fig. 4. There are sequence homologies within protein L25 (Table 6) as well as between protein L25 and other ribosomal proteins (Table 5).Entities:
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Year: 1975 PMID: 1100506 DOI: 10.1515/bchm2.1975.356.2.1343
Source DB: PubMed Journal: Hoppe Seylers Z Physiol Chem ISSN: 0018-4888