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1. Based on the differences in solubility in ammonium sulfate and activity as a function of pH, two L-asparaginases, EC-1 and 2, were partially purified from Escherichia coli 0112. 2. Both L-asparaginases, EC-1 and 2, were highly activated with low concentration of their substrate, L-aspartgine, but inactivated with high concentration of it. 3. Activities of L-asparaginases, EC-1 and 2, were inhibited with the product, L-aspartic acid in proportion to its concentration 4. Both of them were denatured by urea, EC-1 being denatured completely with 6M and EC-2 with 8M urea, showing their spatial conformational difference, since the latter proved to be a little more resistant to urea than the former.
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