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Isolation of thermostable phosphatase from the hyperthermophilic archaeon Thermococcus pacificus by immobilized metal
G E Bannikova1, V P Varlamov, M L Miroshnichenko
1Bioengineering Center, Russian Academy of Sciences, Moscow, Russia.
Biochemistry and Molecular Biology International
|April 8, 1998
Abstract:
Phosphatase was isolated from cells of the hyperthermophilic marine archaeon Thermococcus pacificus by a procedure including chromatography on Butyl-Fractogel TSK-650 and Ni(2+)-iminodiacetic-agarose. Enzyme activity is maximal at 90 degrees C, and the enzyme half-life time at this temperature is 1 h. The pH optimum of phosphatase activity is 6.0. Electrophoresis under denaturating conditions yielded a subunit molecular weight of 45 kDa. On gel-filtration on Sephacryl S-300 HR three peak corresponding to 295, 85 and 45 kDa were observed, suggesting that the enzyme is a homohexamer.