Developing canine retina, fixed in Bouin's or Tellyesnizky's acetic alcoholic formalin, was examined with a battery of biotinylated lectins. ConA and WGA consistently bound to all retinal layers including the tapetum cellulosum, retinal pigment epithelium, inner and outer segments, plexiform layers and ganglion cells. Binding became more intense with increased age. S-WGA bound to apical portions of the retinal pigment epithelium and to outer segments. Outer segments also bound ConA, WGA and RCA. DBA preferentially labelled all inner segments, while PNA bound to a subpopulation of inner segments. RCA bound intensely to retinal vessels as did PNA after neuraminidase treatment. UEA did not consistently bind to any layers. There was transient binding by some lectins at different developmental stages. This study indicates that canine retina demonstrates differential expression of glycoproteins, as indicated by lectin binding, during development and that this expression is temporally and topographically regulated.