| |
Name | Accession
Type | Initial
Conc.
(uM) | Volume
(fL) | Buffered | Sum Total Of |
| 1 | R2C2 | Network | 0.5 | 0 | 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. |
| 2 | R2C2-cAMP | Network | 0 | 0 | No | - |
| | One cAMP bound to site B1 on the regulatory subunits. |
| 3 | R2C2-cAMP2 | Network | 0 | 0 | No | - |
| | One cAMP bound to each of the B sites on the regulatory subunits. |
| 4 | R2C2-cAMP3 | Network | 0 | 0 | No | - |
| | 3 cAMPs now bound. |
| 5 | R2C2-cAMP4 | Network | 0 | 0 | No | - |
| | All the regulatory subunits now have cAMP bound. This state is ready to dissociate and to release the catalytic subunit. |
| 6 | R2C-cAMP4 | Network | 0 | 0 | No | - |
| 7 | R2-cAMP4 | Network | 0 | 0 | No | - |
| | The regulatory subunit with 4 cAMPs but the catalytic subunit has been released. |
| 8 | PKA-inhibitor | Network | 0.25 | 0 | 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. |
| 9 | inhibited-PKA | Network | 0 | 0 | No | - |
| | This is the inhibitor bound to PKA. |
and 
color.