Escherichia Coli의 각종 Isoenzyme에 관한 연구

Abstract

1. Based on the differences in their pH optimas, in solubulities in ammonium sulfate solution, and in the adsorption and elution properties to and from th1 DEAE-cellul08e, L-asparaginases, EC-1 and EC2, were partially purified from Escherκhia coli 0112 Strain. 2. Both partially purified E. coli L-asparaginases. EC-1 and EC•2 , showed such an instability as to have their activities decreased to almost one-half of the original activities during 4 hours incubation at 37°C 3. Activities of the E. coli L-asparaginoses, EC-1 and EC-2, could be enhanced about ten percent by the addition in vitro of the bovine serum albumin and human serum. 4. Activities of the L-asparaginases, EC-1 and EC-2, were inhibited by the product L•aspartic acid , in proportion to its concentration, which was pro tected by the addition of the bovine serum albumin and human serum protein. 5. Since there was observed no difference in their enhancement of activities between EC•1 and EC-2 brought by the non-specific reaction of bovine serum albumin and human serum protein, the protein enhancement of L-asparaginase actirities could not be involved in actitumor effect of the enzyme.