Purification and Characterization of an Acid Phosphatase from Mycoplasma fermentans

Mamoru Noda, Ken Ichiro Shibata, Yoshihiko Sawa, Tsuguo Watanabe, Hirokata Shimokoube

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


An acid phosphatase associated with the cell membranes of Mycoplasma fermentans was released from the membranes with Triton X-100, then purified by ion-exchange chromatography on DEAE-Sephacel and CM-Sepharose, followed by affinity chromatography on Con A-Sepharose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed a single band with a molecular mass of 31.2 kilodaltons. The enzyme activity toward p-nitrophenyl phosphate was enhanced remarkably by Cu2+, Co2+ and Mg2+, but the activity was not inhibited by EDTA. The enzyme dephosphorylated 0-phospho-L-tyrosine as well as p-nitrophenyl phosphate, but not O-phospho-L-threonine, O-phospho-L-serine, glucose-l-phosphate, phosphoryl choline and adenosine triphosphate. The level of the 0-phospho-L-tyrosine phosphatase activity was the highest in Mycoplasma faucium and the second highest in Mycoplasma fermentans of all tested human mycoplasmas.

Original languageEnglish
Pages (from-to)103-107
Number of pages5
Issue number2
Publication statusPublished - Jan 1 1994
Externally publishedYes


  • Acid phosphatase
  • Mycoplasma fermentans

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


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