Biomaterial Database

Sequence determination of protein S9 from the Escherichia coli ribosome. 1977

R Chen

The complete amino acid sequence of ribosomal protein S9 of Escherichia coli has been established. The protein was digested with trypsin and Staphylococcus aureus protease and the resulting peptides were separated by ion exchange chromatography on a new Dowex 50W-X7 microcolumn or a small phosphocellulose column. If necessary, they were rechromatographed on purified cellulose thin-layer plates on a preparative scale. The sequences of the peptides were determined by the micro dansyl-Edman technique, whereas the alignments of the tryptic peptides were mainly established from large cyanogen bromide fragments which were sequenced by the automatic Edman degradation process. Protein S9 is 128 amino acids long and has the following composition: Asx7, Thr5, Ser7, Glx16, Pro3, Gly13, Ala10, Val10, Met3, Ile7, Leu9, Tyr5, Phe4, His1, Lys10, Arg18. The molecular weight as calculated from the amino acid composition is 14 569. A total of 92.6 mg of the lyophilized protein was used for the determination of the primary structure of S9. Most of the material was needed to isolate sufficient amounts of the CNBr-fragments for the automatic degradation in the sequenator.

UI	MeSH Term	Description	Entries
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010447	Peptide Hydrolases	Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.	Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012269	Ribosomal Proteins	Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.	Proteins, Ribosomal,Ribosomal Protein,Protein, Ribosomal
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin