Skip to main content
Log in

Isozymes in nutrient medium of suspension-cultured apple cells (Malus sylvestris Mill.)

  • General Paper
  • Published:
Plant Cell, Tissue and Organ Culture Aims and scope Submit manuscript

Abstract

The time course of the activities of esterase, α-galactosidase, and β-glucosidase in cell sap and nutrient medium in in vitro cultured apple cells (Malus sylvestris Mill.) was studied. The corresponding isozyme patterns and the intracellular and extracellular isozyme patterns of acid phosphatase and polyphenol oxidase were compared using isozyme visualization methods adapted to ultra-thin-layer isoelectric focusing. Neither quantitative (total activity) nor qualitative (isozyme pattern) data were congruent for cell saps and nutrient media. Malate dehydrogenase, malic enzyme, and glutamate dehydrogenase occurred in cell sap only. The extracellular activities probably originate to a great part from a programmed release by intact cells. Nutrient media of plant cell cultures constitute a rich source of active plant isozymes.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Arnison, PG, Boll, WG (1978) The effect of 2.4-D and kinetin on the activity and isozyme pattern of various enzymes in cotyledon cell suspension cultures of bush bean. Can J Bot 56: 2185–2195

    Google Scholar 

  2. Bartley, JM (1974) β-galactosidase activity in ripening apples. Phytochemistry 13: 2109–2111

    Google Scholar 

  3. Berger, RG, Drawert, F, Kinzkofer, A, Kunz, C, Radola, BJ (1985) Proteins and peroxidase in callus and suspension cultures of apple. Plant Physiol 77: 211–214

    Google Scholar 

  4. Bermmeyer, HU (1983) Methods of enzymatic analysis. VCh. Weinheim

    Google Scholar 

  5. Berlin, J, Barz, W (1975) Oxidative decarboxylation of p-hydroxy-benzoic acids by peroxidases. Z Naturforsch 30c: 650–658

    Google Scholar 

  6. Bradford, MM (1977) A rapid sensitive and versatile assay for protein using Coomassie Brilliant Blue G 250. Anal Biochem 79: 544–552

    Google Scholar 

  7. Brakke, MK, Nickell, LG (1951) Secretion of α-amylase by Rumex virus tumors in vitro. Arch Biochem Biophys 32: 28–41

    Google Scholar 

  8. Bredemeijer, GMM, Burg, HCJ, Sree Ramulu, K, Dijkhuis, P (1985) Release of peroxidases by cultured potato cells. Acta Bot Neerl 34: 325–335

    Google Scholar 

  9. Castillo, FJ, Penel, C, Greppin, H (1984) Peroxidase release induced by ozone in Sedum album leaves. Plant Physiol 74: 846–851

    Google Scholar 

  10. Chibbar, RN, VanHuystee, RB (1984) Characterization of peroxidase in plant cells. Plant Physiol 75: 956–958

    Google Scholar 

  11. Gamborg, OL, Eveleigh, DE (1968) Culture methods and detection of glucanases in suspension cultures of wheat and barley. Can J Biochem 46: 417–421

    Google Scholar 

  12. Gaspar, T, Kevers, C, Penel, C, Greppin, H (1983) Auxin control of calcium-mediated peroxidase secretion by auxin-dependent and auxin-independent sugarbeet cells. Phytochemistry 22: 2657–2660

    Google Scholar 

  13. Gomori, G (1953) Human esterases. J Lab Clin Med 42: 44–453

    Google Scholar 

  14. Keegstra, K, Albersheim, P (1970) The involvement of glycosidases in the cell wall metabolism of suspension-cultured Acer pseudoplatanus cells. Plant Physiol 45: 675–678

    Google Scholar 

  15. Kinzkofer, A, Radola, BJ (1983) Fast and high resolution enzyme visualization in ultrathin-layer isoelectric focusing. Electrophoresis 4: 408–417

    Google Scholar 

  16. Maretzki, A, DelaCruz, A, Nickell, LG (1971) Extracellular hydrolysis of starch in sugarcane cell suspensions. Plant Physiol 48: 521–525

    Google Scholar 

  17. Matheis, G, Whitaker, JR (1984) Modification of proteins by polyphenol oxidase and peroxidase and their products. J Food Biochem 8: 137–162

    Google Scholar 

  18. Murashige, T, Skoog, F (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 15: 473–497

    Google Scholar 

  19. Oleson, AE, Janski, AM, Clark, AT (1974) An extracellular nuclease from suspension cultures of tobacco. Biochim Biophys Acta 366: 89–100

    Google Scholar 

  20. Radola, BJ (1980) Ultrathin-layer isoelectric focusing in polyacrylamide gels. Electrophoresis 1: 43–56

    Google Scholar 

  21. Straus, J, Campbell, A (1963) Release of enzymes by plant tissue cultures. Life Sci 2: 50–62

    Google Scholar 

  22. Ueki, K, Sato, S (1971) Effect of inorganic phosphate on the extracellular acid phosphatase activity of tobacco cells cultured in vitro. Physiol Plant 24: 506–511

    Google Scholar 

  23. Van denBerg, BM, VanHuystee, RB (1984) Rapid isolation of plant peroxidase. Physiol Plant 60: 299–304

    Google Scholar 

  24. VanHuystee, RB, Cairns, WL (1982) Progress and prospects in the use of peroxidase to study cell development. Phytochemistry 21: 1843–1847

    Google Scholar 

  25. VanHuystee, RB, Lobarzewski, J (1982) An immunological study of peroxidase release by cultured peanut cells. Plant Sci Lett 27: 59–67

    Google Scholar 

  26. Veliky, I, Sandkvist, A, Martin, SM (1969) Physiology of, and enzyme production by, plant cell cultures. Biotechnol Bioeng 11: 1247–1254

    Google Scholar 

  27. Wetter, L, Dyck, J (1983) Isoenzyme analysis of cultured cells and somatic hybrids. In: Evans, DA, Sharp, WR, Ammirato, PV, Yamada, Y (Eds) Handbook of Plant Cell Culture p 607–628. Macmillan, New York

    Google Scholar 

  28. Widholm, JM (1972) The use of fluorescein diacetate and phenosafranin for determining viability of cultured plant cells. Stain Technol 47: 189–194

    Google Scholar 

  29. Wink, M (1984) Evidence for an extracellular lytic compartment of plant cell suspension cultures. Naturwissenschaften 75: 635–637

    Google Scholar 

  30. Wink, M (1985) Composition of the spent cell culture medium. J Plant Physiol 121: 287–293

    Google Scholar 

  31. Wink, M (1985) Metabolisjm of quinolizidine alkaloids in plants and cell suspension cultures: induction and degradation. In: Neumann, KH, Barz, W, Reinhard, E (Eds) Primary and Secondary Metabolism of Plant Cell Cultures, p 114. Springer, Berlin

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Berger, R.G., Drawert, F. & Kunz, C. Isozymes in nutrient medium of suspension-cultured apple cells (Malus sylvestris Mill.). Plant Cell Tiss Organ Cult 15, 137–147 (1988). https://doi.org/10.1007/BF00035755

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00035755

Key words

Navigation