Cone lamellae and red and green rod outer segment disks contain a large intrinsic membrane protein on their margins: an ultrastructural immunocytochemical study of frog retinas.

In addition to rhodopsin, the disk membranes of rod outer segments (ROS) contain a large integral membrane protein (mol. wt 290,000). This protein was previously localized by immunocytochemistry to the margins and incisures of disks in frog red ROS by specific antibody applied to thin sections of bovine serum albumin embedded retinas (Papermaster et al., 1978b, J. Cell Biol. 78, 415-425). Upon further study of the reactions of this antibody with outer segments of other photoreceptor classes in frog retina, labeling of the short incisures and margins of green ROS and margins of cone outer segment lamellae is also observed. Thus the large protein participates in the structure of the edges of disks and lamellae of all photoreceptors in the frog. In addition, labeling of the inter-incisure surface of all photoreceptor classes was observed at high antibody concentration. In order to interpret this labeling, the effect of dilution on labeling density was determined and double reciprocal plots (Markham and Benton, 1931, J. Am. Chem. Soc. 53, 497) were employed to evaluate the relative affinity and heterogeneity. There was considerable deviation from linearity in the plots of labeling disk interiors compared to the relatively linear plots of disk incisure labeling which suggests that the interior sites contain a weakly cross-reacting antigen or that the serum contains a lower concentration of antibody weakly reactive with another antigen.