Measurement of monovalent and polyvalent carbohydrate-lectin binding by back-scattering interferometry.

ABSTRACT: Carbohydrate-protein binding is important to many areas of biochemistry. Here, backscattering interferometry (BSI) has been shown to be a convenient and sensitive method for obtaining quantitative information about the strengths and selectivities of such interactions. The surfaces of glass microfluidic channels were covalently modified with extravidin, to which biotinylated lectins were subsequently attached by incubation and washing. The binding of unmodified carbohydrates to the resulting avidin-immobilized lectins was monitored by BSI. Dose-response curves that were generated within several minutes and were highly reproducible in multiple wash/measure cycles provided adsorption coefficients that showed mannose to bind to concanavalin A (conA) with 3.7 times greater affinity than glucose

SUBMITTER: Kussrow A 

PROVIDER: S-EPMC2713007 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature