Histochemical study of epididymal secretions in the lizard, Lacerta vivipara. Localization of lectin-binding sites.
The epididymis of lizards elaborates voluminous secretory granules made of a central core and a peripheral vacuole which in the species Lacerta vivipara contain respectively an insoluble protein (protein H) and a soluble protein (protein L). After their discharge these secretions mix with spermatozoa. In order to detect the presence of carbohydrates in these secretions, lectins isolated from Canavalia ensiformis (con A) and from eleven other plants (lentil, soja, pea, gorse and several mushrooms), conjugated to fluorescein isothiocyanate, have been utilized in light-microscopic histochemical investigations of frozen sections from Lacerta vivipara epididymis. Whereas lectins having affinity for L-fucose, lactose, D-galactose and N-acetyl-D-galactosamine bound to central cores, lectins having affinity to D-glucose, N-acetylglucosamine and chitobiose bound to the peripheral vacuole. D-mannose or D-glucose seem to be present both in central cores and in peripheral vacuoles.
D000818:Animals; D003594:Cytoplasmic Granules / Q000378:metabolism; D004822:Epididymis / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D037102:Lectins; D008116:Lizards / Q000033:anatomy & histology / Q000502:physiology*; D008297:Male
D037102:Lectins