Characterisation in situ of the complex carbohydrates in rabbit oviduct using digestion with glycosidases followed by lectin binding.
Enzymatic degradation followed by lectin application was carried out on specimens of the rabbit oviduct. The sequential application of the glycosidases (neuraminidase, alpha-L-fucosidase, beta-galactosidase and alpha-mannosidase) and lectins (peanut, winged pea, wheat germ and soybean) seem promising as an effective method for characterising, in situ, the structure of complex carbohydrate chains. The data obtained after digestion with neuraminidase and alpha-L-fucosidase indicate the presence of a continuous layer of sialoglycoconjugates and fucoglycoconjugates that completely covers the luminal surfaces of the ampulla. The different reactivity of the glycocalyx and the secretory products indicates a different chemical composition of glycoconjugates in the glycocalyx and secretions. Although it is very difficult to explain the lectin affinity and the functional significance of the positive cells, some hypotheses have been advanced.
D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D005187:Fallopian Tubes / Q000378:metabolism*; D005260:Female; D006026:Glycoside Hydrolases; D037102:Lectins / Q000378:metabolism*; D011817:Rabbits / Q000378:metabolism*
D037102:Lectins; D006026:Glycoside Hydrolases