Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodiimide and oligomycin: relationship to ATP synthesis.
Measurement of the rate of [gamma-32P]ATP binding (k1) and release (k-1) from catalytic sites on submitochondrial particles permitted calculation of the affinity constant in catalytic sites (k1 = K1/k1-1) of 10(12) M-1. This value is the same as that determined previously for the solubilized ATPase...
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| Gepubliceerd in: | Proc Natl Acad Sci U S A |
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| Hoofdauteur: | |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
National Academy of Sciences
1985
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC397317/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2858849/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.82.6.1589 |
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