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Kinetics and thermodynamics of the binding of forskolin to the galactose-H+ transport protein, GalP, of Escherichia coli.

The binding of the transport inhibitor, forskolin, to the galactose-H+ symporter, GalP, of Escherichia coli was evaluated by equilibrium and time-resolved fluorescence measurements. A quench in protein fluorescence of 8-12% was observed upon the binding of forskolin. The overall dissociation constan...

Täydet tiedot

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Bibliografiset tiedot
Päätekijät: Martin, G E, Rutherford, N G, Henderson, P J, Walmsley, A R
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 1995
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC1136871/
https://ncbi.nlm.nih.gov/pubmed/7755573
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