Study on RNA N-glycosidase activity of ribosome inactivating proteins Curcin and Curcin C of Jatropha curcas
To investigate the RNA N-glycosidase activity of ribosome inactivating proteins in Jatropha cur-cas,the UPLC-MS/MS method was established to determine the in vitro RNA N-glycosidase depurination activity of Jatropha ribosomal inactivating proteins Curcin and Curcin C.The optimal conditions for the reac-tion of Curcin with RNA32 were 37℃,pH=4.2,and 4 h.For Curcin C reacted with RNA32,the optimal conditions were 37℃,pH=3.7 and 8 h.The Km values of Curcin was 8.231 μmol/L,while that of Curcin C was 3.302 μmol/L,indicating a high affinity of Curcin for the substrate.Some of the metal ions had a pro-motive effect on the enzymatic activity of Curcin C,while all produced inhibition in the case of Curcin.When the adenosine concentration reached 250 μmol/L,the enzyme activity of Curcin C increased,whereas it had no effect on Curcin.When the enzymatic reaction substrates were RNA14 and RNA32,the RNA N-glycosidase activity of Curcin C protein was significantly higher than that of Curcin,indicating that Curcin C has more potential for antitumor drug development compared to Curcin.
Ribosome-inactivating proteinCurcinCurcin CRNA N-glycosidase activityUPLC-MS
国家科技期刊平台
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