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The primary structure of escherichia coli k 12 asparto kinase i ec homo serine dehydrogenase i ec isolation and characterization of the peptides produced by cyanogen bromide/

, : The primary structure of escherichia coli k 12 asparto kinase i ec homo serine dehydrogenase i ec isolation and characterization of the peptides produced by cyanogen bromide/. Biochimica et Biophysica Acta 535(2): 206-215

The aspartokinase I[EC]-homoserine dehydrogenase I [EC] from E. coli K12, composed of four identical subunits of MW 86,000, was carboxymethylated, fragmented by CNBr treatment and citraconylated. Using gel filtration, ion exchange chromatography and preparative paper electrophoresis and chromatography, 15 of 21 CNBr peptides were isolated in pure form and characterized by their composition, their N[amino]-terminal amino acid, and by their content of known cysteinyl or tryptophanyl tryptic peptides.

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