Purification of NADH-Nitrate Reductase by Affinity Chromatography | Zendy

Larry P. Solomonson | Zendy

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Purification of NADH-Nitrate Reductase by Affinity Chromatography

Author(s) -

Larry P. Solomonson

Publication year - 1975

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.56.6.853

Subject(s) - nitrate reductase , chemistry , elution , chromatography , affinity chromatography , agarose , nitrate , ionic strength , oxidoreductase , biochemistry , yield (engineering) , chlorella , electrophoresis , chlorella vulgaris , reductase , enzyme , biology , algae , botany , organic chemistry , materials science , aqueous solution , metallurgy

ASSIMILATORY NITRATE REDUCTASE (NADH: nitrate oxidoreductase, EC 1.6.6.1) from Chlorella vulgaris has been purified to electrophoretic homogeneity with an overall yield of 60% by a procedure that utilizes blue dextran-agarose as an affinity column. Nitrate reductase binds to blue dextran and is not eluted in the presence of high ionic strength buffer but is rapidly eluted in the presence of mumolar concentrations of NADH.

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