Warning: mkdir(): Permission denied in /home/virtual/lib/view_data.php on line 81

Warning: fopen(upload/ip_log/ip_log_2024-09.txt): failed to open stream: No such file or directory in /home/virtual/lib/view_data.php on line 83

Warning: fwrite() expects parameter 1 to be resource, boolean given in /home/virtual/lib/view_data.php on line 84
Phosphate and Carbon Source Regulation of Alkaline Phosphatase and Phospholipase in Vibrio vulnificus
Skip Navigation
Skip to contents

Journal of Microbiology : Journal of Microbiology

OPEN ACCESS
SEARCH
Search

Articles

Page Path
HOME > J. Microbiol > Volume 45(4); 2007 > Article
Research Support, Non-U.S. Gov't
Phosphate and Carbon Source Regulation of Alkaline Phosphatase and Phospholipase in Vibrio vulnificus
Wan-Seok Oh , Young-Sun Im , Kyu-Young Yeon , Young-Jun Yoon , Jung-Wan Kim
Journal of Microbiology 2007;45(4):311-317
DOI: https://doi.org/2567 [pii]
Department of Biology, University of Incheon, Incheon 402-749, Republic of KoreaDepartment of Biology, University of Incheon, Incheon 402-749, Republic of Korea
Corresponding author:  Jung-Wan Kim , Tel: 82-32-770-8244, 
prev next
  • 3 Views
  • 0 Download
  • 0 Crossref
  • 0 Scopus

In this study, the effects of phosphate concentration and carbon source on the patterns of alkaline phosphatase (APase) and phospholipase (PLase) expression in Vibrio vulnificus ATCC 29307 were assessed under various conditions. The activities of these enzymes were repressed by excess phosphate (4 mM) in the culture medium, but this repression was reversed upon the onset of phosphate starvation in low phosphate defined medium (LPDM) containing 0.2 mM of phosphate at approximately the end of the exponential growth phase. The expressions of the two enzymes were also influenced by different carbon sources, including glucose, fructose, maltose, glycerol, and sodium acetate at different levels. The APase activity was derepressed most profoundly in LPDM containing fructose as a sole carbon source. However, the repression/derepression of the enzyme by phosphate was not observed in media containing glycerol or sodium acetate. In LPDM-glycerol or sodium acetate, the growth rate was quite low. The highest levels of PLase activity were detected in LPDMsodium acetate, followed by LPDM-fructose. PLase was not fully repressed by high phosphate concentrations when sodium acetate was utilized as the sole carbon source. These results showed that multiple regulatory systems, including the phosphate regulon, may perform a function in the expression of both or either APase and PLC, in the broader context of the survival of V. vulnificus.

  • Cite this Article
    Cite this Article
    export Copy Download
    Close
    Download Citation
    Download a citation file in RIS format that can be imported by all major citation management software, including EndNote, ProCite, RefWorks, and Reference Manager.

    Format:
    • RIS — For EndNote, ProCite, RefWorks, and most other reference management software
    • BibTeX — For JabRef, BibDesk, and other BibTeX-specific software
    Include:
    • Citation for the content below
    Phosphate and Carbon Source Regulation of Alkaline Phosphatase and Phospholipase in Vibrio vulnificus
    J. Microbiol. 2007;45(4):311-317.
    Close
Related articles

Journal of Microbiology : Journal of Microbiology
TOP