Abstract

The kinetic behavior of glutathione (GSH)/ glutathione-S-transferase (GST) was investigated using surface plasmon resonance (SPR). Here, an alkanethiol-modified chip incorporated with bovine serum albumin (BSA) was employed. Subsequently, GSH was anchored on BSA surface only in the experimental channel and the without-active BSA surface was designed as the reference channel to improve the quality of the binding data and prevent a number of experimental artifacts to complicate the final biosensor analysis. Our results demonstrated that the BSA-modified chip was effective not only in binding the target proteins but also in suppressing the nonspecific binding (NSB) of proteins.

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