Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1996 Nov;112(3):931–938. doi: 10.1104/pp.112.3.931

Immunolocalization of mannitol dehydrogenase in celery plants and cells.

E Zamski 1, Y T Yamamoto 1, J D Williamson 1, M A Conkling 1, D M Pharr 1
PMCID: PMC158020  PMID: 8938403

Abstract

Immunolocalization of mannitol dehydrogenase (MTD) in celery (Apium graveolens L.) suspension cells and plants showed that MTD is a cytoplasmic enzyme. MTD was found in the meristems of celery root apices, in young expanding leaves, in the vascular cambium, and in the phloem, including sieve-element/companion cell complexes, parenchyma, and in the exuding phloem sap of cut petioles. Suspension cells that were grown in medium with mannitol as the sole carbon source showed a high anti-MTD cross-reaction in the cytoplasm, whereas cells that were grown in sucrose-containing medium showed little or no cross-reaction. Gel-blot analysis of proteins from vascular and nonvascular tissues of mature celery petioles showed a strong anti-MTD sera cross-reactive band, corresponding to the 40-kD molecular mass of MTD in vascular extracts, but no cross-reactive bands in nonvascular extracts. The distribution pattern of MTD within celery plants and in cell cultures that were grown on different carbon sources is consistent with the hypothesis that the Mtd gene may be regulated by sugar repression. Additionally, a developmental component may regulate the distribution of MTD within celery plants.

Full Text

The Full Text of this article is available as a PDF (3.2 MB).

Selected References

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

  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Davis J. M., Fellman J. K., Loescher W. H. Biosynthesis of Sucrose and Mannitol as a Function of Leaf Age in Celery (Apium graveolens L.). Plant Physiol. 1988 Jan;86(1):129–133. doi: 10.1104/pp.86.1.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Everard J. D., Franceschi V. R., Loescher W. H. Mannose-6-Phosphate Reductase, a Key Enzyme in Photoassimilate Partitioning, Is Abundant and Located in the Cytosol of Photosynthetically Active Cells of Celery (Apium graveolens L.) Source Leaves. Plant Physiol. 1993 Jun;102(2):345–356. doi: 10.1104/pp.102.2.345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  5. Nolte K. D., Koch K. E. Companion-Cell Specific Localization of Sucrose Synthase in Zones of Phloem Loading and Unloading. Plant Physiol. 1993 Mar;101(3):899–905. doi: 10.1104/pp.101.3.899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Rumpho M. E., Edwards G. E., Loescher W. H. A pathway for photosynthetic carbon flow to mannitol in celery leaves : activity and localization of key enzymes. Plant Physiol. 1983 Dec;73(4):869–873. doi: 10.1104/pp.73.4.869. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Stoop J. M., Williamson J. D., Conkling M. A., Pharr D. M. Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures. Plant Physiol. 1995 Jul;108(3):1219–1225. doi: 10.1104/pp.108.3.1219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Stoop JMH., Pharr D. M. Effect of Different Carbon Sources on Relative Growth Rate, Internal Carbohydrates, and Mannitol 1-Oxidoreductase Activity in Celery Suspension Cultures. Plant Physiol. 1993 Nov;103(3):1001–1008. doi: 10.1104/pp.103.3.1001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Stoop JMH., Pharr D. M. Mannitol Metabolism in Celery Stressed by Excess Macronutrients. Plant Physiol. 1994 Oct;106(2):503–511. doi: 10.1104/pp.106.2.503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Williamson J. D., Stoop J. M., Massel M. O., Conkling M. A., Pharr D. M. Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a function for the pathogenesis-related protein ELI3. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7148–7152. doi: 10.1073/pnas.92.16.7148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Yang N. S., Russell D. Maize sucrose synthase-1 promoter directs phloem cell-specific expression of Gus gene in transgenic tobacco plants. Proc Natl Acad Sci U S A. 1990 Jun;87(11):4144–4148. doi: 10.1073/pnas.87.11.4144. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES