Isolation of thermostable phosphatase from the hyperthermophilic archaeon Thermococcus pacificus by immobilized metal affinity chromatography

Biochem Mol Biol Int. 1998 Feb;44(2):363-70. doi: 10.1080/15216549800201372.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cations, Divalent
  • Chromatography, Affinity / methods*
  • Copper
  • Enzyme Stability
  • Hot Temperature*
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Nickel
  • Phosphoric Monoester Hydrolases / chemistry
  • Phosphoric Monoester Hydrolases / isolation & purification*
  • Phosphoric Monoester Hydrolases / metabolism
  • Thermococcus / enzymology*


  • Cations, Divalent
  • Copper
  • Nickel
  • Phosphoric Monoester Hydrolases