作者: L de Mercoyrol , C Job , D Job
DOI: 10.1042/BJ2580165
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摘要: The rate of formation a single phosphodiester bond with UTP substrate, U-A primer, poly[d(A-T)] template and wheat-germ RNA polymerase II is greatly depressed in the presence alpha-amanitin. Half-maximal inhibition occurs at 0.04 microgram/ml, close agreement published values for productive synthesis class polymerases from higher-plant species. However, sizeable proportion U-A-U resistant to by excess In additional ATP, i.e. under experimental conditions permitting chain elongation, poly[r(A-U)] arrested after first bond. results support contention that main enzymic process disrupted alpha-amanitin translocation step transcription complex along DNA template.