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Partial Purification of the NADH-Nitrate Reductase Complex from Chlorella pyrenoidosa
Author(s) -
Robert H. Schloemer,
Reginald H. Garrett
Publication year - 1973
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.51.3.591
Subject(s) - chlorella pyrenoidosa , nitrate reductase , nitrate , chlorella , chemistry , ammonium , biochemistry , ammonium sulfate , reductase , enzyme , polyethylene glycol , michaelis–menten kinetics , chromatography , fractionation , organic chemistry , biology , enzyme assay , botany , algae
The nitrate reductase complex from Chlorella pyrenoidosa has been purified by a procedure which includes as main steps, ammonium sulfate fractionation, polyethylene glycol treatment, and DEAE-cellulose chromatography. The Michaelis constants for NADH, FAD, and NO(3) (-) in the NADH-nitrate reductase assay are 10 mum, 2.6 mum, and 0.23 mm, respectively. Heat treatment exerts varying effects on the enzymatic activities associated with the nitrate reductase complex.

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