The F1-ATPase from Streptococcus cremoris: isolation, purification and partial characterization.
1. The F1-ATPase from the plasma membrane of Streptococcus cremoris HA was released by low ionic shock wash and purified by gel filtration and ion exchange chromatography. 2. The specific activity of the purified F1-ATPase was 25.8 mumol Pi/mg protein/min. 3. Km for ATP was 0.80 mM, and Ki for ADP as a competetive inhibitor 0.40 mM. 4. The purified F1-ATPase consisted of five subunits, alpha, beta, gamma, delta and epsilon, with molecular masses of 47.0, 45.0, 29.5, 22.0 and 13.0 kDa, respectively. 5. The isoelectric point of the enzyme complex was found to be 4.4.
Rimpiläinen
M A
MA
Department of Biochemistry, University of Oulu, Finland.
Mettänen
T T
TT
Niskasaari
K
K
Forsén
R I
RI
D000244:Adenosine Diphosphate / Q000494:pharmacology; D001667:Binding, Competitive; D002462:Cell Membrane / Q000201:enzymology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007700:Kinetics; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D012995:Solubility; D013291:Streptococcus / Q000201:enzymology*
D000244:Adenosine Diphosphate; D006180:Proton-Translocating ATPases