The amino acid sequence of L-asparaginase [EC 3.5.1.1] from Escherichia coli A-1-3 was studied. Tryptic peptides were purified from S-carboxymethylated asparaginase and their sequences were established by subtractive Edman degradation and enzymatic digestion. The arrangement of the tryptic peptides were deduced from cyanogen bromide peptides of the protein. The sequence indicates that the molecule of L-asparaginase consists of four identical subunits, each with a molecular weight of 34,080.
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Maita et al. (1974) studied this question.
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