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50-S Ribosomal Proteins.
- Source :
- European Journal of Biochemistry; 1972, Vol. 25 Issue 1, p13-19, 7p
- Publication Year :
- 1972
-
Abstract
- Peptide studies on two acidic proteins, A<subscript>1</subscript> and A<subscript>2</subscript>, from 50-S ribosomes of Escherichia coli indicate a closely related primary structure. 1. Amino acid compositions of the tryptic peptides of the two proteins are identical, with exception of the amino terminal peptide. 2. The N-terminal amino acid sequence of A<subscript>2</subscript>-protein is Ser-Ile-Thr-Lys, while that of A<subscript>1</subscript>-protein is N-acetyl-Ser-Ile-Thr-Lys. 3. The estimated number of 120 amino acid residues in each polypeptide chain is consistent with the physical molecular weight estimate. 4. In 50% of the polypeptide chains, in both A<subscript>1</subscript>- or A<subscript>2</subscript>-protein, a specific lysine residue is replaced by ε-N-monomethyl-lysine. [ABSTRACT FROM AUTHOR]
- Subjects :
- PROTEINS
ESCHERICHIA coli
BIOCHEMISTRY
PEPTIDES
AMINO acids
RIBOSOMES
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 25
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13039365