Abstract

Direct and competitive kinetic analysis of the binding between a one domain analogue of protein A, and mutants thereof, to immobilised hIgG1 was compared using a biosensor system based on surface plasmon resonance detection. Rate constants determined from both assays were almost identical. The experiments demonstrate that competitive kinetic analysis can be used in combination with biosensor technology, and indicate that competitive kinetic analysis may extend the use of the technology to include low molecular weight analytes.

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