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.
Expressions of integrated rate equations for enzyme reactions studied in a system where the volume of the medium changes, e.g. with a pH-stat device, are given.
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