Abstract
A surface plasmon resonance imaging method has been developed for high throughput recognition and determination of low level glycoproteins with limited sample volume at least down to 50 nL. Chicken ovalbumin and immunoglobulin G were chosen as model compounds while bovine serum albumin and lysozyme were used as control. Each protein, at a concentration of 0.0080-1.0 mg mL(-1), was printed on one gold sensing film, and the films were simultaneously reacted with a probe solution and viewed using a laboratory-built surface plasmon resonance imaging system. The imaging signals were dependent on the concentration and the type of analyte, with a limit of detection down to at least 0.5 ng. The glycoproteins dotted at either 1.0 mg mL(-1) or 0.010 mg mL(-1) were easily differentiated from the non-glycoproteins by reaction with 200 nM concanavalin A (con A), giving a limit of recognition down also to 0.5 ng glycoprotein. This imaging method was hence considered a new tool for analyzing glycoproteins.
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