Sites of binding of eight different lectins (LTA, UEA I, WGA, SBA, DBA, CON A, PNA, RCA I) to cat submandibular gland were studied after exposure of tissue sections to sialidase, alpha-fucosidase, beta-galactosidase, alpha-mannosidase, beta-N-acetylglucosaminidase. All lectins were affected by enzymatic predigestion and the labeling of individual lectins was highly dependent upon the glycosidase used to pretreat the sections. Glycoconjugates of demilunar, acinar and ductal cells exhibited a different composition of terminal sequences. For example, fucose proved to form the disaccharide fucose-galactose in demilunar and acinar cells, whereas it was present with the sequence fucose-N-acetyl-D-glucosamine in striated duct cells. Sialic acid participated both to the terminal sequence sialic acid-galactose and sialic acid-N-acetyl-D-galactosamine either in demilunar or in ductal cells. Lectin labeling combined with glycosidase digestion was also helpful in verifying the influence of neighbouring oligosaccharides on the affinity of lectins for the respective sugars.

The carbohydrate histochemistry of the rabbit oviduct has been examined by the use of four lectins conjugated with horseradish peroxidase as histochemical reagents. Each lectin gave a very distinct typical pattern of binding, but for each lectin there was no difference between the distribution of binding sites in ampulla and isthmus. Wheat germ lectin bound exclusively with the connective tissue of the oviduct folds; winged pea lectin was detected only in the ciliated cells; peanut lectin binding sites were visualized in the secretory cells; the binding reactivity of soybean lectin was limited to the basal part of the cilia. Although it is very difficult at present to correlate the distribution of lectin binding sites with the function of the positive cells, some hypotheses have been advanced.

The corynebacteria-like microorganisms evoluting in the haemocultures take origin from electron dense granular bodies carried within the erythrocytes.

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