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- W2079748838 abstract "Summary The factor that inactivates the phosphorylated nitrate reductase was purified 870-fold from leaves of Brassica campestris L. ssp. apifera by column chromatography on DEAE-Toyopearl, Phenyl Sepharose, Sephadex G-200 and Mono Q. Final preparation of the purified factor was nearly homogenous as revealed by Polyacrylamide gel electrophoresis and its molecular weight was estimated to be 70 ku using Superose 12 gel filtration column. SDS-polyacrylamide gel analysis of the final preparation showed two protein bands with molecular weight of 30 and 33 ku suggesting that the inactivation factor was composed of two heterogenous subunits. The inactivation of phosphorylated nitrate reductase by the purified protein was neither time dependent, nor due to degradation of nitrate reductase, suggesting that the inactivation factor exhibits its effect by binding to the phosphorylated nitrate reductase." @default.
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- W2079748838 date "1998-01-01" @default.
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- W2079748838 title "Purification of inactivation factor of phosphorylated nitrate reductase from leaves of Brassica campestris" @default.
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- W2079748838 doi "https://doi.org/10.1016/s0176-1617(98)80047-3" @default.
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