Primary Structure of Escherichia coli Glutamine Synthetase
Year: 1971
Type: article
Abstract: A 21-member tryptic peptide containing covalently bound adenylic acid has been isolated by gel filtration and ion exchange chromatography from Escherichia coli glutamine synthetase. The amino acid sequence of the peptide is [see PDF for sequence] Analysis of a thermolysin fragment of the heneicosapeptide containing uniformly labeled 14C-AMP revealed that the radioactivity of the ribose moiety of the AMP is released from the peptide along with tyrosine during the Edman degradation. This establishes that tyrosine is the amino acid residue to which the AMP is covalently bound.
Source: Journal of Biological Chemistry
Authors: Robert L. Heinrikson, Henry S. Kingdon
Institution: University of Chicago
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1517450306