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. 1966 Jan;91(1):1–13. doi: 10.1128/jb.91.1.1-13.1966

Elution of Exocellular Enzymes from Saccharomyces fragilis and Saccharomyces cerevisiae

Ralph Weimberg a,1, William L Orton a
PMCID: PMC315902  PMID: 5903092

Abstract

Weimberg, Ralph (Northern Regional Research Laboratory, Peoria, Ill.), and William L. Orton. Elution of exocellular enzymes from Saccharomyces fragilis and Saccharomyces cerevisiae. J. Bacteriol. 91:1–13. 1966.—Invertase and acid phosphatase are repressible exocellular enzymes in Saccharomyces fragilis and S. cerevisiae. The conditions for eluting these enzymes from both organisms were compared. Either KCl or β-mercaptoethanol eluted the enzymes from S. fragilis, and the amounts eluted varied quantitatively according to the physiological age of the organism. In addition to eluting enzymatic activity from the cells, these reagents also caused a large increase in the amount of activity that remained associated with the cells of S. fragilis. Invertase and acid phosphatase were not removed from cells of S. cerevisiae by KCl or β-mercaptoethanol. These enzymes were separated from S. cerevisiae cells only when there was some degree of cell-wall digestion by snail gut fluid.

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Selected References

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

  1. BURGER M., BACON E. E., BACON J. S. Some observations on the form and location of invertase in the yeast cell. Biochem J. 1961 Mar;78:504–511. doi: 10.1042/bj0780504. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DODYK F., ROTHSTEIN A. FACTORS INFLUENCING THE APPEARANCE OF INVERTASE IN SACCHAROMYCES CEREVISIAE. Arch Biochem Biophys. 1964 Mar;104:478–486. doi: 10.1016/0003-9861(64)90492-8. [DOI] [PubMed] [Google Scholar]
  3. DWORSCHACK R. G., WICKERHAM L. J. Production of extracellular and total invertase by Candida utilis, Saccharomyces cerevisiae, and other yeasts. Appl Microbiol. 1961 Jul;9:291–294. doi: 10.1128/am.9.4.291-294.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DWORSCHACK R. G., WICKERHAM L. J. Production of extracellular invertase by the yeast, Saccharomyces uvarum NRRL Y-972. Arch Biochem Biophys. 1958 Aug;76(2):449–456. doi: 10.1016/0003-9861(58)90170-x. [DOI] [PubMed] [Google Scholar]
  5. HEREDIA C. F., YEN F., SOLS A. Role and formation of the acid phosphatase in yeast. Biochem Biophys Res Commun. 1963 Jan 18;10:14–18. doi: 10.1016/0006-291x(63)90259-6. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. MCLELLAN W. L., Jr, LAMPEN J. O. The acid phosphatase of yeast. Localization and secretion by protoplasts. Biochim Biophys Acta. 1963 Feb 12;67:324–326. doi: 10.1016/0006-3002(63)91832-8. [DOI] [PubMed] [Google Scholar]
  8. NICKERSON W. J. SYMPOSIUM ON BIOCHEMICAL BASES OF MORPHOGENESIS IN FUNGI. IV. MOLECULAR BASES OF FORM IN YEASTS. Bacteriol Rev. 1963 Sep;27:305–324. doi: 10.1128/br.27.3.305-324.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Neu H. C., Heppel L. A. On the surface localization of enzymes in E. coli. Biochem Biophys Res Commun. 1964 Oct 14;17(3):215–219. doi: 10.1016/0006-291x(64)90386-9. [DOI] [PubMed] [Google Scholar]
  10. PARK J. T., JOHNSON M. J. A submicrodetermination of glucose. J Biol Chem. 1949 Nov;181(1):149–151. [PubMed] [Google Scholar]
  11. PHAFF H. J. CELL WALL OF YEASTS. Annu Rev Microbiol. 1963;17:15–30. doi: 10.1146/annurev.mi.17.100163.000311. [DOI] [PubMed] [Google Scholar]
  12. SNYDER H. E., PHAFF H. J. The pattern of action of inulinase from Saccharomyces fragilis on inulin. J Biol Chem. 1962 Aug;237:2438–2441. [PubMed] [Google Scholar]
  13. SUTTON D. D., LAMPEN J. O. Localization of sucrose and maltose fermenting systems in Saccharomyces cerevisiae. Biochim Biophys Acta. 1962 Jan 29;56:303–312. doi: 10.1016/0006-3002(62)90567-x. [DOI] [PubMed] [Google Scholar]
  14. TAUSSKY H. H., SHORR E. A microcolorimetric method for the determination of inorganic phosphorus. J Biol Chem. 1953 Jun;202(2):675–685. [PubMed] [Google Scholar]
  15. WEIMBERG R., ORTON W. L. EVIDENCE FOR AN EXOCELLULAR SITE FOR THE ACID PHOSPHATASE OF SACCHAROMYCES MELLIS. J Bacteriol. 1964 Dec;88:1743–1754. doi: 10.1128/jb.88.6.1743-1754.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. WEIMBERG R., ORTON W. L. REPRESSIBLE ACID PHOSPHOMONOESTERASE AND CONSTITUTIVE PYROPHOSPHATASE OF SACCHAROMYCES MELLIS. J Bacteriol. 1963 Oct;86:805–813. doi: 10.1128/jb.86.4.805-813.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. WICKERHAM L. J., DWORSCHACK R. G. Extracellular invertase production by sexually agglutinative mating types of Saccharomyces kluyveri. Science. 1960 Apr 1;131(3405):985–986. doi: 10.1126/science.131.3405.985. [DOI] [PubMed] [Google Scholar]
  18. WICKERHAM L. J. Evidence of the production of extracellular invertase by certain strains of yeasts. Arch Biochem Biophys. 1958 Aug;76(2):439–448. doi: 10.1016/0003-9861(58)90169-3. [DOI] [PubMed] [Google Scholar]
  19. Weimberg R., Orton W. L. Elution of Acid Phosphatase from the Cell Surface of Saccharomyces mellis by Potassium Chloride. J Bacteriol. 1965 Jul;90(1):82–94. doi: 10.1128/jb.90.1.82-94.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]

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