Abstract
We have previously produced a polyclonal antiserum (R 1S 5) against a plasma membrane-enriched fraction of rat retinal pigment epithelial (RPE) cells which inhibits the phagocytosis of photoreceptor outer segments (OS) by these cells. This antiserum has now been used to purify a subset of RPE membrane glycoproteins. Using a combination of lectin affinity chromatography, and chromatography on an affinity column made with R 1S 5-IgG, we have enriched an RPE membrane extract about 100-fold. This enriched extract contains only 12 components, all of which are glycoproteins, and retains the ability to adsorb out the inhibitory activity of antiserum R 1S 5. This shows that one or more of these glycoproteins recognizes an inhibitory IgG in R 1S 5and suggests that one or more of these glycoproteins may participate in the phagocytosis of OS by RPE cells, possibly as the phagocytosis receptor. We have performed N-terminal microsequencing of seven of these glycoproteins: four of the seven, with M rs of 34, 36, 51 and 55 kDa, show no sequence homology to any known proteins.
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