Purification and characterization of ATPase from Nitrobacter winogradskyi.
An ATPase was purified from Nitrobacter winogradskyi, and some of its molecular and enzymatic properties were determined. The enzyme was composed of two subunits of 64 and 59 kDa, respectively. The enzyme had its pH optimum at 9.5 and showed a specific activity of 7 units per mg protein. This activity was about 14% and 18% of that of F1-ATPases obtained from Escherichia coli and Sulfolobus acidocaldarius, respectively. The enzyme was 29% and 6% inhibited by 100 microM dicyclohexylcarbodiimide (DCCD) and 100 microM NaN3, respectively. It was not inhibited by 20 mM NaNO3.
Hara
T
T
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Villalobos
A P
AP
Fukumori
Y
Y
Yamanaka
T
T
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D001386:Azides / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009576:Nitrobacter / Q000201:enzymology*; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D019810:Sodium Azide
D001386:Azides; D004024:Dicyclohexylcarbodiimide; D019810:Sodium Azide; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases