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From the
1 From the Microbiology Department, Scripps Clinic and Research Foundation, La Jolla, California 92037
Radioactivity incorporated into an
Tryptophan Synthetase ß2 Subunit
PRIMARY STRUCTURE OF THE PYRIDOXYL PEPTIDE FROM THE ESCHERICHIA COLI ENZYME
-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].
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