title: Lectin binding sites in the vitelline envelope of Bufo arenarum oocytes: role in fertilization.
abstract: Incubation of dejellied spawned oocytes from Bufo arenarum with different lectins results in a decrease of oocyte fertility. Concanavalin A was the most effective lectin; phytohemagglutinin P and wheat germ lectin were less effective. Agglutinin from soybean was scarcely active. These lectin effects could be ascribed to a hindering of specific sites for some proteases, since the same treatment renders the oocyte vitelline envelope insensitive to spermatolysin (an essential requisite for fertilization) and to trypsin. Also in this case concanavalin A was the most effective lectin. Univalent concanavalin A was also effective in blocking the fertility of dejellied oocytes. These results indicate that the residues of alpha-D-glucose and alpha-D-mannose present in the vitelline envelope are involved in gamete interactions in Bufo arenarum. This idea is also supported by the finding that dejellied oocytes (fertilizables) have a number of binding sites for concanavalin A that is three or four orders of magnitude higher than coelomic or fertilized oocytes (both not penetrable by spermatozoa).
authors.affiliation: Departamento de Biología del Desarrollo, Universidad Nacional de Tucumán, San Miguel de Tucumán, Argentina.
authors.forename: E J
authors.initials: EJ
authors.lastname: del Pino
authors.forename: M O
authors.initials: MO
authors.lastname: Cabada
mesh_terms: D000818:Animals; D002022:Bufo arenarum; D005260:Female; D005298:Fertility; D005306:Fertilization; D009865:Oocytes / Q000187:drug effects / Q000276:immunology / Q000502:physiology*; D010447:Peptide Hydrolases / Q000494:pharmacology; D011952:Receptors, Concanavalin A / Q000502:physiology; D011975:Receptors, Mitogen / Q000502:physiology*; D014817:Vitelline Membrane / Q000276:immunology / Q000502:physiology*
chemical_list: D011952:Receptors, Concanavalin A; D011975:Receptors, Mitogen; D010447:Peptide Hydrolases