Skip to main content
Log in

Subcellular localization of acid proteinase in barley mesophyll protoplasts

  • Short Communication
  • Published:
Planta Aims and scope Submit manuscript

Abstract

Chloroplasts prepared from lysed protoplasts of barley mesophyll contain 2–8% of the total acid proteinase activity. This residual activity is not associated with intact chloroplasts isolated by means of density gradient centrifugation. Vacuoles isolated from lysed protoplasts contain 80–85% of the total acid proteinase activity, indicating that the enzyme(s) which is presumably responsible for the degradation of chloroplastic proteins is located largely in the central vacuoles of mesophyll cells.

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.

References

  • Arnon, D.I. (1949) Copper enzymes in isolated chloroplasts; polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1–15

    Google Scholar 

  • Boller, Th., Kende, H. (1979) Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 63, 1123–1132

    Google Scholar 

  • Hampp, R., DeFilippis, L.F. (1980) Plastid protease activity and prolamellar body transformation during greening. Plant Physiol. 65, 663–668

    Google Scholar 

  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275

    PubMed  Google Scholar 

  • Martinoia, E., Heck, U., Wiemken, A.: (1980) The vacuoles as storage compartments for nitrate in barley leaves. Nature (London) (in press)

  • Matile, Ph (1975) The lytic compartment of plant cells. Cell Biology Monographs, vol. 1, Springer-Verlag, Wien New York

    Google Scholar 

  • Peoples, M.B., Dalling, M.J. (1979) Intracellular localization of acid peptide hydrolases in wheat leaves. Plant Physiol. suppl. 63/5 p. 159, abstract Nr. 882

    Google Scholar 

  • Peterson, L.W., Huffaker, R.C. (1975) Loss of ribulose 1.5-diphosphate carboxylase and increase in proteolytic activity during senescence of detached primary barley leaves. Plant Physiol. 55, 1009–1015

    Google Scholar 

  • Ragster, L., Chrispeels, M.J. (1979) Azocoll-digesting proteinases in soybean leaves. Characteristics and changes during leaf maturation and senescence. Plant Physiol. 64, 857–862

    Google Scholar 

  • Spector, Th. (1978) Refinement of the Coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for ≦0.5 to 50 μg of protein. Ann. Biochem. 86, 142–146

    Google Scholar 

  • Wittenbach, V.A. (1978) Breakdown of ribulose biphosphate carboxylase and change in proteolytic activity during dark-induced senescence of wheat seedlings. Plant Physiol. 62, 604–608

    Google Scholar 

  • Yemm, E.W., Cocking, E.C. (1955) The determination of amino acids with ninhydrin. Analyst (Lond.) 80, 209–213

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Heck, U., Martinoia, E. & Matile, P. Subcellular localization of acid proteinase in barley mesophyll protoplasts. Planta 151, 198–200 (1981). https://doi.org/10.1007/BF00387823

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00387823

Key words

Navigation