Vacuolar-Type ATPase in a Hyperthermophilic Archaeum,Thermococcussp. KI

• Published in: Biochemical and biophysical research communications Vol. 229; no. 2; pp. 559 - 564
• Main Authors: Iida, Toshii, Hoaki, Toshihiro, Kamino, Kei, Inatomi, Ken-ichi, Kamagata, Yoichi, Maruyama, Tadashi
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 13.12.1996

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...