Skip to main content
Log in

Secretion of β-glucosidase by Ochromonas danica

  • Published:
Archives of Microbiology Aims and scope Submit manuscript

Abstract

β-Glucosidase released by the phytoflagellate Ochromonas danica was the result of secretion; this was adduced from the following: (1) The enzyme was released during growth, including early log phase. (2) The amount released was calculated to be much more than could be attributed to cell lysis. (3) β-Glucosidase was released by cells during short term incubation in a dilute salt solution; this release was nearly linear for at least 24 h. (4) Release occurred while cell counts remained nearly constant and cells remained viable. (5) Control experiments excluded cell damage resulting from incubation and cell manipulation as a source of the exoenzyme. (6) No alkaline phosphatase was released and 5 times less phosphoglucose isomerase than glucosidase was released while the cells contained 7 times more phosphoglucose isomerase. (7) The kinetics of release of nonspecific protein and UV absorbing material was markedly different from glucosidase release. (8) Glucosidase release was temperature and energy dependent; anaerobiosis decreased enzyme release. (9) Release was inhibited by cycloheximide. (10) Cells incubated with 3H-leucine synthesized labeled protein which was secreted linearly for at least 24h. Cycloheximide inhibited incorporation of 3H-leucine into protein and the secretion of the labeled protein.

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

Abbreviations

CHI:

cycloheximide

DNP:

2,4-dinitrophenol

IAA:

iodoacetic acid

PGI:

phosphoglucose isomerase

SIS:

salt incubation solution

References

  • Aaronson, S.: Digestion in phytoflagellates. In: Lysosomes in biology and pathology, Vol. 3 (J. T. Dingle, H. B. Fell, eds.), pp. 18–37. London: North-Holland 1973

    Google Scholar 

  • Aaronson, S., Baker, H.: A comparative biochemical study of two species of Ochromonas. J. Protozool. 6, 282–284 (1959)

    Google Scholar 

  • Aronson, N. N., Jr., deDuve, C.: Digestive activity of lysosomes. II. The digestion of macromolecular carbohydrates by extracts of rat liver lysosomes. J. biol. Chem. 243, 4564–4573 (1968)

    Google Scholar 

  • Bauduin, H., Colin, M., Dumont, J. E.: Energy sources for protein synthesis and enzymatic secretion in rat pancreas in vitro. Biochim. biophys. Acta (Amst.) 174, 722–733 (1969)

    Google Scholar 

  • Bessey, O. A., Lowry, O. H., Brock, M. J.: A method for the rapid determination of alkaline phosphatase with five cubic millimeters of serum. J. biol. Chem. 164, 321–329 (1946)

    Google Scholar 

  • Biely, P., Farkas, V., Bauer, S.: Secretion of β-glucanase by Saccharomyces cerevisiae protoplasts. FEBS Letters 23, 153–156 (1972)

    Google Scholar 

  • Dingle, J. T.: The extracellular secretion of lysosomal enzymes. In: Lysosomes in biology and pathology, Vol. 2 (J. T. Dingle, H. B. Fell, eds.), pp. 421–436. London: North-Holland 1969

    Google Scholar 

  • Gomori, G.: Preparation of buffers for use in enzyme studies. In: Methods in enzymology, Vol. 1 (S. P. Colowick, N. O. Kaplan, eds.), pp. 138–146. New York Academic Press 1955

    Google Scholar 

  • Hartree, E. F.: Determination of protein: A modification of the Lowry method that gives a linear photometric response. Analyt. Biochem. 48, 422–427 (1972)

    Google Scholar 

  • Jamieson, J. D., Palade, G. E.: Condensing vacuole conversion and zymogen granule discharge in pancreatic exocrine cells: Metabolic studies. J. Cell Biol. 48, 503–522 (1971)

    Google Scholar 

  • Lampen, J. O.: Secretion of enzymes by micro-organisms. In: Function and structure in microorganisms, 15th Symp. Soc. Gen. Microbiol. (M. R. Pollock, M. A. Richmond, eds.), pp. 115–133. England: Cambridge University Press 1964

    Google Scholar 

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

    Google Scholar 

  • Muller, M.: Digestion. In: Protozoa, Vol. 1 (G. W. Kidder, ed.), pp. 351–377, New York: Academic Press 1967

    Google Scholar 

  • Muller, M.: Secretion of acid hydrolases and its intracellular source in Tetrahymena puriformis. J. Cell Biol. 52, 478–487 (1972)

    Google Scholar 

  • Patni, N. J., Aaronson, S.: Partial characterization of the intra-and extracellular acid phosphatase of an alga, Ochromonas danica. J. gen. Microbiol. 83, 9–20 (1974)

    Google Scholar 

  • Pollock, M. R.: Exoenzymes. In: The bacteria, Vol. 4 (I. C. Gunsalus, R. Y. Stanier, eds.), pp. 121–178. New York: Academic Press 1962

    Google Scholar 

  • Reithel, F. J.: Phosphoglucose isomerase. II. Mammary gland. In: Methods in enzymology, Vol. 9 (S. P. Colowick, N. O. Kaplan, eds.), pp. 565–568 New York: Academic Press 1966

    Google Scholar 

  • Van Rijn, H. J. M., Boer, P., Steyn-Parve, E. P.: Biosynthesis of acid phosphatase of bakers yeast. Factors influencing its production by protoplasts and characterization of the secreted enzyme. Biochim. biophys. Acta (Amst.) 268, 431–441 (1972)

    Google Scholar 

  • Rogers, H. J.: The dissimilation of high molecular weight substances. In: The bacteria, Vol 2 (I. C. Gunsalus, R. Y. Stanier, eds.), pp. 257–302, New York: Academic Press 1961

    Google Scholar 

  • Rothstein, T. L., Blum, J. J.: Lysosomal physiology in Tetrahymena. I. Effect of glucose, acetate, pyruvate and carmine on intracellular content and extracellular release of three acid hydrolases. J. Cell Biol. 57, 630–641 (1973)

    Google Scholar 

  • Rothstein, T. L., Blum, J. J.: Lysosomal physiology in Tetrahymena. II. Effect of culture age and temperature on the extracellular release of three acid hydrolases. J. Protozool. 21, 163–168 (1974)

    Google Scholar 

  • Stewart, J. E., Schotz, M. C.: Studies on release of lipoprotein lipase activity from fat cells. J. biol. Chem. 246, 5749–5753 (1971)

    Google Scholar 

  • Varner, J. E., Mense, R. M.: Characteristics of the process of enzyme release from secretory plant cells. Plant Physiol. 49, 187–189 (1972)

    Google Scholar 

  • Zurier, R. B., Hoffstein, S., Weissmann, G.: Mechanisms of lysosomal enzyme release from human leukocytes. I. Effect of cyclic nucleotides and colchicine. J. Cell Biol. 58, 27–41 (1973)

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Meyer, D.H. Secretion of β-glucosidase by Ochromonas danica . Arch. Microbiol. 109, 263–270 (1976). https://doi.org/10.1007/BF00446637

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00446637

Key words

Navigation