Purification and some properties of the nitrate reductase from Ankistrodesmus braunii
- 1 February 1976
- journal article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 17 (1) , 1-10
- https://doi.org/10.1093/oxfordjournals.pcp.a075247
Abstract
Purification of the nitrate reductase from Ankistrodesmus braunii to homogeneity is described. The Km values are 0.19 mu for NO3−, 0.75mM for FMNH2, 4μM for methyl viologen, 11 μM for NADH and 30 μM for NADPH. Azide thiocyanate and nitrite inhibit the enzyme reaction competitively. Ki values for these compounds are 7.8 × 10−7, 1.2×10−5 and 4×10−4M respectively. The molecular weight of the intact enzyme determined by disc electrophoresis is 475,000 and that of its subunit 60,000 daltons. Difference spectra of the enzyme show the involvement of cytochrome in nitrate reduction.Keywords
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