This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Arnold, W. N. Search for Related Content PubMed PubMed Citation Articles by Arnold, W. N.

 Previous Article  |  Next Article 

J Bacteriol. 1972 December; 112(3): 1346-1352
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Location of Acid Phosphatase and ß-Fructofuranosidase Within Yeast Cell Envelopes

¹ Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66103

ABSTRACT

After 16 hr of incubation in a low-phosphate, aerated medium, bakers' yeast was obtained with a high titer of acid phosphatase (EC 3.1.3.2) and ß-fructofuranosidase (EC 3.2.1.26). All of the ß-fructofuranosidase and 75% of the acid phosphatase were easily released by mechanical disruption in a French pressure cell. The cell wall suffered a limited number of cracks, but this was sufficient for the co-release of these enzymes. Both enzymes were subject to autolytic release, although correlation was inconclusive because of the relative instability of acid phosphatase. The data are consistent with the bulk of the two enzymes being located in the periplasmic space. Ethylacetate treatments yielded ghosts with high ß-fructofuranosidase but low acid phosphatase activities. The surviving acid phosphatase was not representative of that in live cells. It was resistant to release by mechanical disruption and showed a high susceptibility to heat inactivation. The ß-fructofuranosidase in live cells and in ethylacetatetreated cells exhibited polydispersity in heat inactivation susceptibility; but the kinetics were indistinguishable, and facile release by mechanical disruption was shown in both cases.

This article has been cited by other articles:

• Bernard, M., Mouyna, I., Dubreucq, G., Debeaupuis, J.-P., Fontaine, T., Vorgias, C., Fuglsang, C., Latge, J.-P. (2002). Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus. Microbiology 148: 2819-2829 [Abstract] [Full Text]