Two-dimensional gel electrophoretic analysis of lectin receptors in the bovine interphotoreceptor matrix.

Proteins and glycoproteins of the bovine interphotoreceptor matrix (IPM) with or without neuraminidase treatment was analysed by two-dimensional gel electrophoresis combined with Western blotting and staining with seven horseradish peroxidase-labeled lectins. More than 80 spots of proteins and glycoproteins were revealed on the gel. Nineteen spots (or groups of spots) were revealed by staining with five lectins [concanavalin A, wheat germ agglutinin (WGA), peanut agglutinin (PNA), Ricinus communis agglutinin-1 (RCA-1) and soybean agglutinin (SBA)]; some of those spots were specific for one lectin and others reacted with several lectins. We could not detect distinct spots reacting with Dolichos biflorus agglutinin or Ulex europaeus agglutinin-1. Neuraminidase digestions of the IPM increased and unmasked the binding spots for PNA, RCA-1 and SBA. The spots of WGA-receptors without neuraminidase treatment were mostly identical to the receptors for PNA, RCA-1 and SBA, which became prominent after the digestion. Spots reacting with RCA-1 were mostly identical to the spots of SBA-receptors. The spots reacting with PNA coincided only partially with the spots reacting with RCA-1 and SBA.