E. coli K-12 w 1485의 exponential phase와 stationary phase에서 얻은 glucose-6-phosphate dehydrogenase의 차이점을 관찰하여 다음과 같은 결과를 얻었다. 1) Exponential phase의 E. coli K-12로 부터 추출한 효소는 stationary phase의 E. coli K-12로 부터 추출한 효소보다도 열에 대한 안정도가 높았다. 2) Exponential phase에서 얻은 효소는 stationary phase에서 얻은 효소보다 disc gel electrophoresis에서 빠른 이동도를 나타내었다. 3) Exponential phase와 stationary phase에서 얻은 각각의 효소는 5~25% sucrose gradient ultracentrifugation 및 Sephadex G-200 Column chromatography에서 차이점을 찾지 못하였다. 4) Exponential 및 stationary phases에서 얻은 효소의 NADP에 대한 Km 값은 각각 $0.59{ imes}10^{-4}M$과 $1.3{ imes}10^{-4}M$이였으며 glucose-6-phosphate에 대한 Km 값은 각각 $2.2{ imes}10^{-4}M$과 $1.3{ imes}10^{-4}M$이였다. 5) 두 효소의 최적 pH는 8.0이 였다.
The differences of glucose-6-phosphate dehydrogenase of E. coli K-12 w 1485 at exponential phase and at stationary phase were studied, and the following results were obtained. 1) Heat stability of glucose-6-phosphate dehydrogenase from E. coli K-12 at exponential phase was higher than that of glucose-6-phosphate dehydrogenase from E. coli K-12 at stationary phase. 2) Mobility of the enzyme from exponential phase was faster than that from stationary phase. 3) No difference was observed between the enzyme from exponential phase and stationary phase in 5-25% sucrose density gradient ultracentrifugation and sephadex G-200 chromatograph. 4) KM values of the enzymes from exponential and stationary phases for NADP were $0.59{ imes}10^{-4}M$ and $1.3{ imes}10^{-4}M$, respectively. And Km values for glucose-6-phosphate were $2.2{ imes}10^{-4}M$ and $1.3{ imes}10^{-4}M$. 5) Optimum pH was 8.0 for the both enzymes.
