Partial Purification of the L-Asparaginase from Escherichia Coli and a Study on its Enzymatic Properties.
- Author:
Ro Jung PAK
1
Author Information
1. Department of Urology, and Biochemistry, College of Medicine, Seoul National University, Seoul, Korea.
- Publication Type:Original Article
- Keywords:
l-Asparaginase;
Escherichia;
coli
- MeSH:
Ammonium Sulfate;
Aspartic Acid;
Escherichia coli*;
Escherichia*;
Hydrogen-Ion Concentration;
Solubility;
Urea
- From:Korean Journal of Urology
1973;14(3):155-163
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
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.
