| | Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| 1 | inhibited-PKA | 0 | 0.09 | No |
| | |
| 2 | PKA-active | 0 | 0.09 | No |
| | |
| 3 | PKA-inhibitor | 0.2593 | 0.09 | No |
| | About 25% of PKA C subunit is dissociated in resting cells without having any noticable activity. Doskeland and Ogreid Int J biochem 13 pp1-19 suggest that this is because there is a corresponding amount of inhibitor protein. |
| 4 | R2-cAMP4 | 0 | 0.09 | No |
| | Starts at 0.15 for the test of fig 6 in Smith et al, but we aren't using that paper any more. |
| 5 | R2C-cAMP4 | 0 | 0.09 | No |
| | |
| 6 | R2C2 | 0.5 | 0.09 | No |
| | This is the R2C2 complex, consisting of 2 catalytic (C) subunits, and the R-dimer. See Taylor et al Ann Rev Biochem 1990 59:971-1005 for a review. The Doskeland and Ogreid review is better for numbers. Amount of PKA is about .5 uM. |
| 7 | R2C2-cAMP | 0 | 0.09 | No |
| | CoInit was .0624 |
| 8 | R2C2-cAMP2 | 0 | 0.09 | No |
| | |
| 9 | R2C2-cAMP3 | 0 | 0.09 | No |
| | |
| 10 | R2C2-cAMP4 | 0 | 0.09 | No |
| | |
