Fluorescence energy transfer between ATPase monomers in sarcoplasmic reticulum reconstituted vesicles, in the presence of low concentrations of a nonionic detergent.
We measured fluorescence energy transfer between ATPase monomers labeled with either a donor or an acceptor fluorophore, in order to test the hypothesis that the presumably oligomeric sarcoplasmic reticulum ATPase would dissociate into monomers within the membrane on the addition of low nonsolubilizing amounts of a nonionic detergent, C12E18. We found that at low nonsolubilizing detergent concentrations below the critical micellar concentration (c.m.c.), there was indeed direct interaction between the detergent and the protein; however, only solubilizing detergent concentrations reduced fluorescence transfer to a minimum. Considering the current literature, fluorescence energy transfer proved insufficient, at the present time, to confirm or reject the hypothesis.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D003902:Detergents / Q000494:pharmacology*; D004735:Energy Transfer; D005456:Fluorescent Dyes; D007700:Kinetics; D011092:Polyethylene Glycols / Q000494:pharmacology*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D013501:Surface-Active Agents / Q000494:pharmacology*
D003902:Detergents; D005456:Fluorescent Dyes; D013501:Surface-Active Agents; C017272:dodecyloctaethyleneglycol monoether; D011092:Polyethylene Glycols; D000251:Adenosine Triphosphatases