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PMID: 1100506 Published · ppublish English Journal Article

The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes.

Hoppe-Seyler's Zeitschrift fur physiologische Chemie ·Vol. 356 ·No. 9 ·1975-09-00 ·Pages 1343-52

Bitar KG, Wittmann-Liebold B

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).

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Escherichia coli/analysis Peptide Fragments/analysis Protein Binding RNA, Ribosomal Ribosomal Proteins/analysis Ribosomes/analysis Thermolysin Trypsin
Chemicals
Amino Acids Peptide Fragments RNA, Ribosomal Ribosomal Proteins Trypsin Thermolysin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bitar K G
Wittmann-Liebold B
Article Info
Journal
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Abbr.
Hoppe Seylers Z Physiol Chem
ISSN
0018-4888
Published
1975-09-00
Pages
1343-52
Language
English
Region
Germany
NLM ID
2985060R
Subset
IM
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