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. 2005 Nov;79(21):13806–13810. doi: 10.1128/JVI.79.21.13806-13810.2005

FIG. 1.

FIG. 1.

The binding of aptamer to gp120 is independent of N-linked glycosylation. (A) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the endo H-treated deglycosylated gp120. The molecular mass (∼63 kDa) of the endo H-treated gp120, which is reduced compared to that of the mock-treated gp120 (∼92 kDa) indicates near-complete deglycosylation of the native glycoprotein. (B-D) Overlay of BIAcore sensorgrams to show the binding of the indicated analytes to glycosylated (solid line) and deglycosylated (dashed line) Ba-L monomeric gp120 immobilized on a CM5 biosensor chip. The signal from a control cell for each analyte (dotted line) has been subtracted from all sensorgrams in this and subsequent figures. The horizontal I-shaped bars show the injection period of the analytes. RU, response units; SPR, surface plasmon resonance.