| | Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| 1 | inhibited-PKA | 0 | 1000 | No |
| | |
| 2 | PKA-inhibitor | 0.25 | 1000 | No |
| | |
| 3 | R2-cAMP4 | 0 | 1000 | No |
| | |
| 4 | R2C-cAMP4 | 0 | 1000 | No |
| | R-dimer bound to 4 cAMP molecules. |
| 5 | R2C2 | 0.5 | 1000 | No |
| | PKA: Protein kinase activated by cAMP.
R2C2 complex consists of 2 catalytic (C) subunits, and the R-dimer. There are two types of cAMP binding sites termed A and B according to the rate with which they exchange bound labelled nucleotide.
Dagfinn Ogreid and Stein Ove Doskeland (1981) Int.J.Biochem. 13(1):1-19
Physiological concentration of PKA = 0.59 uM (cardiac myocyte)
Jeffrey J. Saucerman et al (2003) J.Biol.Chem. 278(48):47997-48003 |
| 6 | R2C2-cAMP | 0 | 1000 | No |
| | R2C2 complex consisting of 2 catalytic (C) subunits, and the R-dimer with one molecule of cAMP bound to site B1 on the regulatory subunit. |
| 7 | R2C2-cAMP2 | 0 | 1000 | No |
| | R2C2 complex consisting of 2 catalytic (C) subunits, and the R-dimer with one molecule of cAMP bound to each of the B sites on the regulatory subunit. |
| 8 | R2C2-cAMP3 | 0 | 1000 | No |
| | R2C2 complex consisting of 2 catalytic (C) subunits, and the R-dimer with 3 cAMP molecules bound to it. |
| 9 | R2C2-cAMP4 | 0 | 1000 | No |
| | R2C2 complex consisting of 2 catalytic (C) subunits, and the R-dimer with 4 cAMP molecules bound to it. All the regulatory subunits now have cAMP bound. This state is ready to dissociate and to release the catalytic subunit. |
