Purification and Characterization of an Acid Phosphatase from <i>Mycoplasma fermentans</i>

• Noda Mamoru

  Department of Oral Bacteriology, Hokkaido University School of Dentistry|Department of Operative Dentistry, Hokkaido University School of Dentistry

• Shibata Ken-ichiro

  Department of Oral Bacteriology, Hokkaido University School of Dentistry

• Sawa Yoshihiko

  Department of Oral Bacteriology, Hokkaido University School of Dentistry

• Shimokoube Hirokata

  Department of Operative Dentistry, Hokkaido University School of Dentistry

• Watanabe Tsuguo

  Department of Oral Bacteriology, Hokkaido University School of Dentistry

抄録

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 O-phospho-L-tyrosine as well as p-nitrophenyl phosphate, but not O-phospho-L-threonine, O-phospho-L-serine, glucose-1-phosphate, phosphoryl choline and adenosine triphosphate. The level of the O-phospho-L-tyrosine phosphatase activity was the highest in Mycoplasma faucium and the second highest in Mycoplasma fermentans of all tested human mycoplasmas.

収録刊行物

• MICROBIOLOGY and IMMUNOLOGY

  MICROBIOLOGY and IMMUNOLOGY 38 (2), 103-107, 1994

  Center For Academic Publications Japan

詳細情報

• CRID: 1573950403012621056
• NII論文ID: 130007312224
• ISSN: 03855600
• Web Site: http://chemport.cas.org/cgi-bin/sdcgi?APP=ftslink&action=reflink&origin=jstage2&version=1.0&coi=1:CAS:528:DyaK2cXmsV2jtb8%3D&md5=189c3d9283d1a7fba678426378139281
• 本文言語コード: en
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