title: Inheritance of nitrite reductase and regulation of nitrate reductase, nitrite reductase, and glutamine synthetase isozymes.
abstract: Banding patterns of nitrate reductase (NR), nitrite reductase (NiR), and glutamine synthetase (GS) from leaves of diploid barley (Hordeum vulgare), tetraploid wheat (Triticum durum), hexaploid wheat (Triticum aestivum), and tetraploid wild oats (Avena barbata) were compared following starch gel electrophoresis.  Two NR isozymes, which appeared to be under different regulatory control, were observed in each of the three species.  The activity of the more slowly migrating nitrate reductase isozyme (NR1) was induced by NO3- in green seedlings and cycloheximide inhibited induction.  However, the activity of the faster NR isozyme (NR2) was unaffected by addition of KNO3, and it was not affected by treatments of cycloheximide or chloramphenicol.  Only a single isozyme of nitrite reductase was detected in surveys of three tetraploid and 18 hexaploid wheat, and 48 barley accessions; however, three isozymes associated with different ecotypes were detected in the wild oats.  Inheritance patterns showed that two of the wild oat isozymes were governed by a single Mendelian locus with two codominant alleles; however, no variation was detected for the third isozyme.  Treatment of excised barely and wild oat seedlings with cycloheximide and chloramphenicol showed that induction of NiR activity was greatly inhibited by cycloheximide, but only slightly by chloramphenicol.  Only a single GS isozyme was detected in extracts of green leaves of wheat, barley, and wild oat seedlings.  No electrophoretic variation was observed within or among any of these three species.  Thus, this enzyme appears to be the most structurally conserved of the three enzymes.
authors.affiliation: Department of Agronomy and Range Science, University of California, Davis 95616, USA.
authors.forename: S
authors.initials: S
authors.lastname: Heath-Pagliuso
authors.forename: R C
authors.initials: RC
authors.lastname: Huffaker
authors.forename: R W
authors.initials: RW
authors.lastname: Allard
mesh_terms: D018554:Avena / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D002701:Chloramphenicol / Q000494:pharmacology; D003513:Cycloheximide / Q000494:pharmacology; D018506:Gene Expression Regulation, Plant; D005974:Glutamate-Ammonia Ligase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001467:Hordeum / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009565:Nitrate Reductases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D009566:Nitrates / Q000494:pharmacology; D009572:Nitrite Reductases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D018515:Plant Leaves / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology / Q000235:genetics; D017680:Potassium Compounds / Q000494:pharmacology; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D014908:Triticum / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics
chemical_list: D007527:Isoenzymes; D009566:Nitrates; D017680:Potassium Compounds; D011500:Protein Synthesis Inhibitors; D002701:Chloramphenicol; D003513:Cycloheximide; D009565:Nitrate Reductases; D009572:Nitrite Reductases; D005974:Glutamate-Ammonia Ligase; C023844:potassium nitrate