Evidence for a plasma-membrane-bound nitrate reductase involved in nitrate uptake of Chlorella sorokiniana

Anti-nitrate-reductase (NR) immunoglobulin-G (IgG) fragments inhibited nitrate uptake into Chlorella cells but had no affect on nitrite uptake. Intact anti-NR serum and preimmune IgG fragments had no affect on nitrate uptake. Membrane-associated NR was detected in plasma-membrane (PM) fractions isol...

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Bibliographic Details
Published in:Planta 1989, Vol.178 (1), p.19-24
Main Authors: Tischner, R., Ward, M.R., Huffaker, R.C.
Format: Article
Language:English
Subjects:
Antiserum
Barley
Biological and medical sciences
Biological Transport
Cell Membrane - enzymology
Cell membranes
Chlorella - cytology
Chlorella - metabolism
Chlorella - physiology
Chlorella - ultrastructure
Cytosol - enzymology
Enzymes
Fundamental and applied biological sciences. Psychology
Immune Sera - immunology
Immune Sera - pharmacology
Immunoglobulin G - pharmacology
Man/System Technology And Life Support
Metabolism
Nitrate Reductases - analysis
Nitrate Reductases - antagonists & inhibitors
Nitrate Reductases - physiology
Nitrates
Nitrates - pharmacokinetics
Nitrites
Nitrogen metabolism
Oxidation-Reduction
Plant cells
Plant physiology and development
Plant roots
Plants
Quaternary ammonium compounds
Solubility
Space life sciences
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Summary:Anti-nitrate-reductase (NR) immunoglobulin-G (IgG) fragments inhibited nitrate uptake into Chlorella cells but had no affect on nitrite uptake. Intact anti-NR serum and preimmune IgG fragments had no affect on nitrate uptake. Membrane-associated NR was detected in plasma-membrane (PM) fractions isolated by aqueous two-phase partitioning. The PM-associated NR was not removed by sonicating PM vesicles in 500 mM NaCl and 1 mM ethylenediaminetetraacetic acid and represented up to 0.8% of the total Chlorella NR activity. The PM NR was solubilized by Triton X-100 and inactivated by Chlorella NR antiserum. Plasma-membrane NR was present in ammonium-grown Chlorella cells that completely lacked soluble NR activity. The subunit sizes of the PM and soluble NRs were 60 and 95 kDa, respectively, as determined by sodium-dodecyl-sulfate electrophoresis and western blotting.
ISSN:0032-0935
1432-2048
DOI:10.1007/BF00392522