The Primary Structure of L-Asparaginase fromEscherichia coli

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Abstract
The carboxymethylated L-asparaginase from E. coli A-1-3 was fragmented with cyanogen bromide and the resulting peptides were isolated by using gel filtration on Sephadex G-50 and column chromatography on DE-52. The amino acid sequences of the 7 cyanogen bromide peptides thus obtained were established completely or partially by further fragmentation with trypsin, chymotrypsin and pepsin, and the Dansyl Edman method. Based on the above results and the complete sequences of the tryptic peptides from the carboxymethylated L-asparaginase reported in a previous paper, the whole sequence of the enzyme was established. The reported sequence consists of 321 amino acid residues and its calculated MW is 34,080.