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. 2000 Mar 7;97(7):3195–3200. doi: 10.1073/pnas.050558397

Table 2.

Energy transfer measurements and calculated values

Samples* Quench (E) P values Separation, Å % Monomers Turnover, min−1§
Purified ATPase (10) 0.6260  ± 0.0315 49.6  ± 1.1 0 9,690  ± 340
Microsomes (19) 0.2822  ± 0.0287 <0.0001 63.1  ± 1.2 53.3  ± 4.6 9,473  ± 397
Microsomes, no phalloidin (10) 0.3378  ± 0.0338 60.4  ± 1.1 47.6  ± 5.4 9,476  ± 420
Microsomes + phalloidin (9) 0.2202  ± 0.0397 0.0183 66.7  ± 2.1 61.6  ± 6.3 9,470  ± 363

*Numbers in parentheses are number of FRET experiments. Values given in the table are the means ± standard error of the mean. 

The P values were determined by using an unpaired, one-tailed t-test. 

% Monomers were determined by assuming the purified ATPase was 100% dimer and dividing the energy transfer efficiency (E) of the microsomes by E (0.626) of the purified ATPase. 

§Turnover values for purified ATPase are the mean ± SD from ref. 16. Turnover values for microsomes are the mean ± SD from three experiments ± phalloidin.