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- W1877505497 abstract "A nitrate reductase-inactivator protein has been purified 16,000-fold from spinach leaves by pH 5 treatment, chromatography on SE53, Con A-Sepharose, and chromatofocusing. The yield was 12%, the specific activity was 115 units mg−1. Polyacrylamide gel electrophoresis of the final purified inactivator fraction yielded 2 major protein bands and both bands exhibited nitrate reductase-inactivator activity. Analysis of this inactivator protein by gel filtration and SDS-gel electrophoresis revealed protein stainable material only in a molecular weight range of 110,000–115,000. SDS gel electrophoresis under reducing conditions yielded 2 protein bands corresponding to molecular weights of 51,000 and 53,000. The proteolytic mapping for the two separated subunits appeared similar and possibly identical." @default.
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- W1877505497 date "1992-06-01" @default.
- W1877505497 modified "2023-09-23" @default.
- W1877505497 title "A Nitrate Reductase Inactivator Protein from Spinach. Purification, Molecular Weight and Subunit Composition" @default.
- W1877505497 doi "https://doi.org/10.1093/oxfordjournals.pcp.a078263" @default.
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