Vacuolar-Type ATPase in a Hyperthermophilic Archaeum,Thermococcussp. KI
Membrane ATPase was purified from a hyperthermophilic heterotrophic archaeum,Thermococcussp. KI, which grew anaerobically at 90°C in the presence of sulfur. The purified enzyme had an optimal temperature of 90°C and its molecular mass was estimated to be 600 kDa. It consisted of 4 subunits with mole...
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Published in | Biochemical and biophysical research communications Vol. 229; no. 2; pp. 559 - 564 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
13.12.1996
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Online Access | Get full text |
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