Binding of lectins to L4. (A) For each lectin, 4, 20 and 100 ng were spotted in triplicate. One set of a total of four sets is shown in the figure. Spots in rows A-C, columns 1–3 contained H. pomatia lectin (HPA), rows A-C, columns 4–6 contained T. vulgare lectin (WGA), rows D-F, columns 1–3 contained B. simplicifolia B4 (BS) and rows D-F, columns 4–6 contained C. ensiformis lectin (ConA). The slide was incubated with 2% gelatin to block non-specific sites. Biotin-tagged peptide was incubated with the slide and then the amount of peptide bound was detected by binding of Cy3-conjugated streptavidin and measuring fluorescence of the spots. In columns marked B, buffer A was spotted as blanks. (B) Biotin-tagged L4 or control peptide was bound in wells of a streptavidin-coated microtiter plate. The wells were blocked with 2% gelatin, washed, and then equal amounts (50 ng) of lectins conjugated with peroxidase were added. After washing, the amount of lectin bound was detected by peroxidase activity. Standard curves were determined with each lectin-peroxidase conjugate to quantitate binding. Data are expressed as the amount of lectin bound minus a blank without peptide. Light blue bars, peptide L4; dark blue bars, control peptide.