| Popis: |
1. 1. Suncus murinus was injected dibutyryl adenosine 3′,5′-cyclic monophosphate (Bt 2 cAMP) and assayed serine-glyoxylate aminotransferase (EC 2.6.1.45) and serine dehydratase (EC 4.2.1.13). 2. 2. Serine dehydratase was induced 4-fold by Bt 2 cAMP. The K m values of the induced enzyme for l -serine and pyridoxal 5′-phosphate was 57 mM and 3.0 μM, respectively. The enzyme had a pH optimum at pH 10.0. These kinetic properties and pH optimum were same as those of the enzyme from the control. Both the holoenzyme and the apoenzyme increased to the same extent by Bt 2 cAMP. 3. 3. Serine-glyoxyate aminotransferase activity was decreased slightly by the Bt 2 cAMP injection. The holoenzyme activity was increased, but the apoenzyme decreased. K m values for l -serine and glyoxylate of this enzyme were 6mM and 0.2 mM, respectively, without change by Bt 2 cAMP. |
