Premium
LECTIN RECEPTORS ON ROD AND CONE MEMBRANES
Author(s) -
Bridges C. D. B.,
Fong S.L.
Publication year - 1980
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1980.tb03791.x
Subject(s) - lectin , receptor , rhodopsin , chemistry , membrane , biochemistry , glycoprotein , mannose , agglutination (biology) , biophysics , biology , antigen , retinal , genetics
— The oligosaccharides of rod and cone membranes were investigated with the aid of fluorescence and 125 I‐labeled lectins. Additionally, the ability of lectins to cause agglutination in rod outer segment (ROS) suspensions was used as an index for the presence of the corresponding lectin receptors. The specificities of lectin‐ligand interactions were determined from studies of inhibition by various haptene sugars. The membranes of both rods and cones have receptors for Con A, PNA, RCA‐120, RCA‐60, SBA and WGA. The affinity of PNA for accessory cones is much higher than for the principal cones. There do not appear to be receptors for UeA and LTA on rods or cones. Additionally, receptors for HPA and DBA were identified on ROS. These results suggest the existence of the following sugar residues: The binding of Con A and WGA to ROS membrane proteins electrophoresed on SDS‐polyacrylamide gels was also investigated. In addition to rhodopsin, these lectins also bind to the 291000‐dalton protein, indicating that it is a glycoprotein containing mannose and GlcNAc.