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J. Biochem, 1974, Vol. 76, No. 6 1351-1354
© 1974 Japanese Biochemical Society

research-article

Amino Acid Sequence of L-Asparaginase from Escherichia coli

Tetsuo MAITA, Kazuko MOROKUMA and Genji MATSUDA1

Department of Biochemistry, Nagasaki University, School of Medicine Nagasaki, Nagasaki 852

1To whom request for reprints should be addressed

The amino acid sequence of L-asparaginase [EC 3.5.1.1 [EC] ] 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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