The Primary Structure of Bacillus subtilis Acidic Ribosomal Protein B-L9Isolation and Characterization of Peptides and the Complete Amino Acid Sequence
- 1 April 1980
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 87 (4) , 1185-1201
- https://doi.org/10.1093/oxfordjournals.jbchem.a132852
Abstract
The complete primary structure of Bacillus subtilis acidic protein B-L9, functionally equivalent to protein L7/L12 from E. coli has been determined. B-L9 is composed of 122 residues and has the amino acid composition: Asp3, Asn3, Thr4, Ser8, Glu22, Gln1, Pro3, Gly11, Ala21, Val14, Ile2, Leu12, Phe2, Lys13, and Arg1. The molecular weight of B-L9 is 12,633. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequenator, and micro dansyl-Edman degradation of the peptides obtained from digestions with trypsin, thermolysin, Staphylococcus aureus protease, chymotrypsin and pepsin. A comparison of protein B-L9 from B. subtilis with E-L12 from E. coli shows a relatively high degree of homology.This publication has 0 references indexed in Scilit: