| Value |
0.07
mM
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Kent RB, Guterman SK. Pyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity. Proc Natl Acad Sci U S A. 1982 Jul 79(13):3992-6.PubMed ID6125940
|
| Method |
Preparation of p and Assay of ATPase, [tritium]Poly(C) Binding Assay, Kinetic Measurements, Pyrophosphatase Assays, Protein Determination, |
| Comments |
The Ki for inhibition of p ATPase activity by PPi was determined
from experiments as shown in Fig. 3. For wild-type
rho, researchers obtained a Ki of 0.074 ± 0.004 mM (five experiments),
whereas rho-115 p had a Ki of 0.072 + 0.013 mM (seven experiments). |
| Entered by |
Uri M |
| ID |
104787 |