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Can I read Purification, Stabilization and Characterization of Nitrite Reductase from Barley Roots on EtoBox?

Purification, Stabilization and Characterization of Nitrite Reductase from Barley Roots by Shoji Ida; Eigo Mori; Yuhei Morita is a Agricultural and Biological Sciences article available to read on EtoBox.

What is Purification, Stabilization and Characterization of Nitrite Reductase from Barley Roots about?

Nitrite reductase (NiR) isolated from barley (Hordeum vulgare L.) roots was stabilized in a buffer solution containing a sulfhydryl-reducing reagent and glycerol. The enzyme was purified 340fold by ammonium sulfate fractionation and chromatography on DEAE-Sephadex A-50, Sephadex G-200 and DEAE-cellulose. Purified NiR had a specific activity of 28 μmol NO2 (-) reduced min(-1) mg(-1) of protein. The purified preparation was reddishbrown having absorption maxima at 282, 388 and 577 nm. The barley-root enzyme was almost identical with spinach-leaf NiR with respect to molecular weight, isoelectric point, pH stability, pH optimum, affinity for substrate, behavior toward inhibitors. It is concluded that NiR is the same enzymatic entity regardless of its localization in photosynthetic or nonchlorophyllous tissues. The electron-transport system for NiR in root tissue is discussed in comparison with that in leaf tissue.

Who reads Purification, Stabilization and Characterization of Nitrite Reductase from Barley Roots?

It is typically read by researchers, students, and practitioners in Agricultural and Biological Sciences.

Author
Shoji Ida; Eigo Mori; Yuhei Morita
Publisher
Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc. (ISSN 0032-0935)
Published
1974
Language
EN
Field
Agricultural and Biological Sciences (Life Sciences)

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