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 Cu
2+, Co
2+ and Mg
2+, 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.
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