The effect of anionic detergents on the ATPase activity of isolated F1 from the thermophilic bacterium PS3.
The ATPase activity of F1 isolated from the thermophilic bacterium PS3 is stimulated at 30 degrees C by the anionic detergents cholate or deoxycholate. Maximal activity obtained with these detergents (35 mumol/min X mg) is similar to the activity reported for the optimal temperature, 75 degrees C. The activity is linearly stimulated by the detergents and maximal activity is obtained at the critical micellar concentration of the respective detergent. The results are discussed in relation to the role of subunit interactions of the oligomeric enzyme during catalysis and the mode of interaction between the subunits.
Norling
B
B
D001419:Bacteria / Q000201:enzymology*; D019826:Cholic Acid; D002793:Cholic Acids / Q000494:pharmacology; D003080:Cold Temperature; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology*; D007700:Kinetics; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology; D011136:Polysorbates / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013501:Surface-Active Agents / Q000494:pharmacology*
D002793:Cholic Acids; D003902:Detergents; D011136:Polysorbates; D013501:Surface-Active Agents; D003840:Deoxycholic Acid; D011092:Polyethylene Glycols; D017830:Octoxynol; D006180:Proton-Translocating ATPases; D019826:Cholic Acid