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

European journal of biochemistry ·Vol. 139 ·No. 2 ·1984-03-01 ·Pages 225-34

Kimura M, Chow CK

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%.

MeSH Terms

Amino Acid Sequence Bacterial Proteins/isolation & purification Chemical Phenomena Chemistry Escherichia coli/analysis Geobacillus stearothermophilus/analysis Protein Conformation Ribosomal Protein S9 Ribosomal Proteins/isolation & purification

Chemicals

Bacterial Proteins Ribosomal Protein S9 Ribosomal Proteins ribosomal protein L17 ribosomal proteins L27

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Kimura M

Chow C K

Article Info

Journal

European journal of biochemistry

Abbr.

Eur J Biochem

ISSN

0014-2956

DOI

10.1111/j.1432-1033.1984.tb07998.x

Published

1984-03-01

Pages

225-34

Language

English

Region

England

NLM ID

0107600

Subset

External Links

PubMed source DOI: 10.1111/j.1432-1033.1984.tb07998.x

Analysis Services

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

Contact

WeChat Official Account