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Tryptophan Synthetase ß2 Subunit

PRIMARY STRUCTURE OF THE PYRIDOXYL PEPTIDE FROM THE ESCHERICHIA COLI ENZYME

Rudolf Fluri 1, L. E. Jackson 1, W. E. Lee 1, and I. P. Crawford 1

From the 1 From the Microbiology Department, Scripps Clinic and Research Foundation, La Jolla, California 92037

Radioactivity incorporated into an egr-N-5'-phosphopyridoxyllysine residue of the ß chain by reduction of the ß2 holoenzyme with tritiated sodium borohydride appears in two tryptic peptides. These pyridoxyl peptides differ by only a single arginyl residue. As expected, tryptic digests of normal protein contain two peptides that together make up the pyridoxyl peptide region. The primary structure in this region was determined to be: [see PDF for sequence].

Submitted on April 9, 1971


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