The Amino‐Acid Sequence of the Dihydrofolate Reductase of a Trimethoprim‐Resistant Strain of Escherichia coli

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Abstract
The determination of the amino acid sequence of the dihydrofolate reductase from Escherichia coli RT500 is described. The sequence, comprising 159 residues, has been derived from automatic sequencing of the intact protein in conjunction with manual sequencing of lysine‐blocked tryptic peptides, Staphylococcus aureus protease peptides, and α‐lytic protease peptides. Comparison of the sequence with that of the dihydrofolate reductase from a methotrexate‐resistant strain of E. coli (MB1428) shows that 145 of the residues are identical. The distribution of the differences along the length of the molecule is discussed.