| | Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| 1 | I1 | 1.8 | 1000 | No |
| | I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-competitive, so it just turns the enzyme off without interacting with the binding site. Cohen et al 1989 Ann rev Biochem 58:453-508 refer to results where concentration of the inhibitor is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM. |
| 2 | I1* | 0.001 | 1000 | No |
| | Phosphorylated form of the inhibitor. This has a high affinity for the PP1 catalytic subunit. Upon binding the PP1 is inactivated. Cohen 1989 Ann Rev Biochem 58:453-508 |
| 3 | PP1-I1 | 0 | 1000 | No |
| | This form is bound to the non-phosphorylated inibitory subunit and is prone to dissociate. Cohen 1989 Ann Rev biochem 58:453-508 |
| 4 | PP1-I1* | 0 | 1000 | No |
| | This form has the inibitory fragment phosphorylated. The binding of PP1 is tight when the inhibitory fragment is phosphorylated Cohen 1989 Ann Rev Biochem 58:453-508 |
