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-cellu
Purification and properties of nitrite reductase from roots of pea (Pisum sativumcv. Meteor)
โ Scribed by Caroline G. Bowsher; Michael J. Emes; R. Cammack; Dereck P. Hucklesby
- Publisher
- Springer-Verlag
- Year
- 1988
- Tongue
- English
- Weight
- 684 KB
- Volume
- 175
- Category
- Article
- ISSN
- 0032-0935
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โฆ Synopsis
Nitrite reductase (EC 1.6.6.4) prepared from pea roots was found to be immunologically indistinguishable from pea leaf nitrite reductase. Comparisons of the pea root enzyme with nitrite reductase from leaf sources showed a close similarity in inhibition properties, light absorption spectrum, and electron paramagnetic resonance signals. The resemblances indicate that the root nitrite reductase is a sirohaem enzyme and that it functions in the same manner as the leaf enzyme in spite of the difference in reductant supply implicit in its location in a non-photosynthetic tissue.
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