Investigation of luminal surface structures of rod photoreceptor outer segments by lectin cytochemistry combined with freeze-etching.

The luminal surface of the rod photoreceptor disk membrane was exposed by means of osmotic shock and labeled with ferritin- conjugated concanavalin A. The structural changes of the luminal surface were examined by a freeze-etching procedure with cryoprotectant (methanol). On replicas from freeze-etched membranes with concanavalin A labeling, 6- to 10-nm particles were codistributed with ferritin particles on the luminal surface of the disk membrane. By contrast, there were few ferritin particles or less numerous 6- to 10-nm particles on the corresponding surface without concanavalin A labeling. If 6- to 10-nm particles corresponded to the carbohydrate moiety of rhodopsin, concanavalin A binding might tend to preserve this carbohydrate moiety. These results suggest that the two-dimensional analysis of lectin-induced structural changes of the membrane surface glycoconjugates may become available by lectin cytochemistry combined with freeze-etching.