Trypsin peptide patterns of tryptophan synthase beta2 protein among four species of the Enterobacteriaceae

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Abstract
The tryptophan synthase .beta.2 protein (EC 4.2.1.20) of Escherichia coli, Enterobacter aerogenes, Serratia marcescens and Erwinia carotovora was purified and compared. Two-dimensional total peptide patterns for 4 .beta.2 proteins obtained after digestion with trypsin showed that approximately 3/4 of the total peptides are common to all 4 peptides. Examination of only arginine-containing peptides showed that approximately 1/2 of these peptides are common. From a comparative standpoint, the data provide evidence that the primary structure of .beta.2 proteins is relatively similar, indicating that the trpB cistron is evolutionarily conserved in the enteric bacteria group.