Article
Subtle differences in dissociation rates of interactions between destabilized human carbonic anhydrase II mutants and immobilized benzenesulfonamide inhibitors probed by a surface plasmon resonance biosensor.
Analytical biochemistry - 15 Sept 2001
Svedhem S, Enander K, Karlsson M, Sjöbom H, Liedberg B, Löfås S, Mårtensson L G, Sjöstrand S E, Svensson S, Carlsson U, Lundström I
Abstract excerpt
The development of commercial biosensors based on surface plasmon resonance has made possible careful characterization of biomolecular interactions. Here, a set of destabilized human carbonic anhydrase II (HCA II) mutants was investigated with respect to their interaction kinetics with two different immobilized benzenesulfonamide inhibitors. Point mutations were located distantly from the active site, and the...
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