A newly discovered enzyme, that can catalyze the formation of phosphotriester/-diester bonds between nucleic acids, was found to be associated with plant and animal viruses; （i.e. southern bean mosaic virus, brome mo...A newly discovered enzyme, that can catalyze the formation of phosphotriester/-diester bonds between nucleic acids, was found to be associated with plant and animal viruses; （i.e. southern bean mosaic virus, brome mosaic virus, influenza virus, avian virus and mouse retrovirus）. A partially purified enzyme from maize developing endosperms was prepared through 15%-35% ammonium sulfate fractionation, DEAE-cellulose anion exchange column chromatography and Sephadex GI50 gel filtration. The enzyme preparation was then used to demonstrate its main functional characteristics. The enzyme can use varieties of short and long chain length of nucleotides as substrates. However, the enzyme requires at least a minimum of 3 to 4 units of nucleotide chain length for the reaction to occur. The enzyme activity shows an optimum reaction in 50 mM sodium acetate buffer at pH 5.4 and is significantly inhibited by 6-azauridine as compared to other nucleotide analogs. By analyzing the data documented in literature and the results from the present study of the association of this enzyme with viruses and the distinctive inhibitory effect of 6-azauridine, it is speculated that this enzyme is likely associated with many other plant and animal viruses. The association of this enzyme on the surface of virus particles can be explored as a common antigen for developing a versatile antiviral vaccine.展开更多
文摘A newly discovered enzyme, that can catalyze the formation of phosphotriester/-diester bonds between nucleic acids, was found to be associated with plant and animal viruses; （i.e. southern bean mosaic virus, brome mosaic virus, influenza virus, avian virus and mouse retrovirus）. A partially purified enzyme from maize developing endosperms was prepared through 15%-35% ammonium sulfate fractionation, DEAE-cellulose anion exchange column chromatography and Sephadex GI50 gel filtration. The enzyme preparation was then used to demonstrate its main functional characteristics. The enzyme can use varieties of short and long chain length of nucleotides as substrates. However, the enzyme requires at least a minimum of 3 to 4 units of nucleotide chain length for the reaction to occur. The enzyme activity shows an optimum reaction in 50 mM sodium acetate buffer at pH 5.4 and is significantly inhibited by 6-azauridine as compared to other nucleotide analogs. By analyzing the data documented in literature and the results from the present study of the association of this enzyme with viruses and the distinctive inhibitory effect of 6-azauridine, it is speculated that this enzyme is likely associated with many other plant and animal viruses. The association of this enzyme on the surface of virus particles can be explored as a common antigen for developing a versatile antiviral vaccine.
