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- W186579427 abstract "In vitro transcription study under conditions where 5S ribosomal (rRNA) synthesis was highly active in oocyte extracts of X. laevis, the transcriptional activity was not detected in oocyte extracts of cold treated R. catesbiana. The lack of 5S rRNA transcription was not due to the absence of RNA polymerase III, since this enzyme was still active when poly d(A-T) was used as a template. It was found that R. catesbiana extracts could cleave exogenously added 5S rRNA, tRNA and VA-RNA while the X. laevis extract could not. The presence of this RNase activity was not a result of oocyte destruction because eggs derived from R. catesbiana oocytes, which contained this RNase activity, developed into tadpoles after artificial fertilization. In order to elucidate the relationship between the RNase activity and the regulation of gene transcription of cold treated R. catesbiana, this enzyme was purified to homogeneity and characterized. This enzyme could be inactivated by heating to 80C for 15 min, but was resistant to acid and alkaline conditions. The optimal temperature for activity was 55C-65C, while the optimal pH was 4 in 50 mM acetate buffer and 8 in 50 mM Tris-buffer. The optimal cation concentration for the enzyme activity wasmore » 4 mM and 0.5 mM for Mg{sup ++} and Zn{sup ++} respectively. The specific cleavage site of this enzyme was located at the phosphodiester bond to the 3{prime} side of the pyrimidine in the pyrimidine-p-G segment. The antiserum against the purified RNase was prepared and used for quantitating this enzyme under different condition.« less" @default.
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- W186579427 date "1991-03-11" @default.
- W186579427 modified "2023-09-26" @default.
- W186579427 title "Purification and characterization of RNase from Rana catesbiana (bullfrog) oocytes" @default.
- W186579427 hasPublicationYear "1991" @default.
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