Article
Fluorescence and NMR investigations on the ligand binding properties of adenylate kinases.
Biochemistry - 14 Aug 1990
Reinstein J, Vetter I R, Schlichting I, Rösch P, Wittinghofer A, Goody R S
Abstract excerpt
A new system for measurement of affinities of adenylate kinases (AK) for substrates and inhibitors is presented. This system is based on the use of the fluorescent ligand alpha,omega-di[(3' or 2')-O-(N-methylanthraniloyl)adenosine-5'] pentaphosphate (mAP5Am), which is an analogue of the bisubstrate inhibitor diadenosine pentaphosphate (AP5A). It allows the determination of dissociation constants for any ligand in...
Topics
- Adenylate Kinase
- Binding Sites
- Binding, Competitive
- Enzyme Stability
- Escherichia coli
- Fluorescence
- Fluorescent Dyes
- Kinetics
- Ligands
- Magnetic Resonance Spectroscopy
- Mutation