Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1976 Jul;58(1):12–16. doi: 10.1104/pp.58.1.12

Influence of Temperature on Nitrate Metabolism and Leaf Expansion in Soybean (Glycine max L. Merr.) Seedlings 1

Antonio C Magalhães a,2, Doyle B Peters a, Richard H Hageman a
PMCID: PMC542170  PMID: 16659611

Abstract

The effect of various day temperatures on NADH-nitrate reductase, NADH- and NADPH-glutamate dehydrogenases, nitrate, protein and leaf area, measured at intervals during the ontogeny of the first trifoliolate soybean leaf, was determined. At 32.5 C and 25 C, nitrate concentration, nitrate reductase, and NADPH-glutamate dehydrogenase activities increased concurrently with leaf development and then decreased as leaf maturation progressed. At 40 C, these three components showed no initial increase and the concentration or activities decreased throughout the development of the leaf. The effects of temperature on NADH-glutamate dehydrogenase were the reverse. Rates of protein accumulation were higher at 40 C during the first 2 days of leaf development while higher rates were measured the first 5 days of leaf growth at 32.5 C. At 25 C, protein accumulation was low during the first 3 days of leaf growth, increased in the period of 3 to 5 days, and then declined up to 8 days of leaf development. Leaf expansion progressed at faster rates at 32.5 C and 25 C and at a much slower rate at 40 C. Leaf growth was essentially complete after the fifth day regardless of temperature.

In crude leaf homogenates, apparent irreversible inactivation temperatures were 36 C for nitrate reductase and 65 C for NADPH-glutamate dehydrogenase. In vivo studies indicated a lower inactivation temperature for NADPH-glutamate dehydrogenase; however, it was still more heat-tolerant than nitrate reductase.

We envisaged that reduced nitrogen supplied by NO3− assimilation is a factor in leaf expansion.

Full text

PDF
12

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arnon D. I. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949 Jan;24(1):1–15. doi: 10.1104/pp.24.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. FORTI G., TOGNOLI C., PARISI B. Purification from pea leaves of a phosphatase that attacks nucleotides. Biochim Biophys Acta. 1962 Aug 13;62:251–260. doi: 10.1016/0006-3002(62)90038-0. [DOI] [PubMed] [Google Scholar]
  3. Ferrari T. E., Yoder O. C., Filner P. Anaerobic nitrite production by plant cells and tissues: evidence for two nitrate pools. Plant Physiol. 1973 Mar;51(3):423–431. doi: 10.1104/pp.51.3.423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Harper J. E. Canopy and Seasonal Profiles of Nitrate Reductase in Soybeans (Glycine max L. Merr.). Plant Physiol. 1972 Feb;49(2):146–154. doi: 10.1104/pp.49.2.146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Harvey R. B. ENZYMES OF THERMAL ALGAE. Science. 1924 Nov 21;60(1560):481–482. doi: 10.1126/science.60.1560.481. [DOI] [PubMed] [Google Scholar]
  6. Joy K. W. Glutamate dehydrogenase changes in lemna not due to enzyme induction. Plant Physiol. 1971 Mar;47(3):445–446. doi: 10.1104/pp.47.3.445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Joy K. W. Nitrogen metabolis of Lemna minor. II. Enzymes of nitrate assimilation and some aspects of their regulation. Plant Physiol. 1969 Jun;44(6):849–853. doi: 10.1104/pp.44.6.849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Lea P. J., Miflin B. J. Alternative route for nitrogen assimilation in higher plants. Nature. 1974 Oct 18;251(5476):614–616. doi: 10.1038/251614a0. [DOI] [PubMed] [Google Scholar]
  10. Leech R. M., Kirk P. R. An NADP-dependent L-glutamate dehydrogenase from chloroplasts of Vicia faba L. Biochem Biophys Res Commun. 1968 Aug 21;32(4):685–690. doi: 10.1016/0006-291x(68)90293-3. [DOI] [PubMed] [Google Scholar]
  11. Magalhaes A. C., Neyra C. A., Hageman R. H. Nitrite assimilation and amino nitrogen synthesis in isolated spinach chloroplasts. Plant Physiol. 1974 Mar;53(3):411–415. doi: 10.1104/pp.53.3.411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Massey V., Curti B., Ganther H. A temperature-dependent conformational change in D-amino acid oxidase and its effect on catalysis. J Biol Chem. 1966 May 25;241(10):2347–2357. [PubMed] [Google Scholar]
  13. Miflin B. J. The location of nitrite reductase and other enzymes related to amino Acid biosynthesis in the plastids of root and leaves. Plant Physiol. 1974 Oct;54(4):550–555. doi: 10.1104/pp.54.4.550. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. O'Neal D., Joy K. W. Glutamine synthetase of pea leaves. I. Purification, stabilization, and pH optima. Arch Biochem Biophys. 1973 Nov;159(1):113–122. doi: 10.1016/0003-9861(73)90435-9. [DOI] [PubMed] [Google Scholar]
  15. Pahlich E., Joy K. W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. Can J Biochem. 1971 Jan;49(1):127–138. doi: 10.1139/o71-018. [DOI] [PubMed] [Google Scholar]
  16. Schrader L. E., Ritenour G. L., Eilrich G. L., Hageman R. H. Some characteristics of nitrate reductase from higher plants. Plant Physiol. 1968 Jun;43(6):930–940. doi: 10.1104/pp.43.6.930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wells G. N., Hageman R. H. Specificity for nicotinamide adenine dinucleotide by nitrate reductase from leaves. Plant Physiol. 1974 Aug;54(2):136–141. doi: 10.1104/pp.54.2.136. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES