Localization of yolk proteins and their possible precursors using polyclonal and monoclonal antibodies, in Helix aspersa.
Three major yolk proteins of 140, 100, 80 KD and a faint band of 440 KD were determined by gradient gel electrophoresis in the mature eggs of Helix aspersa. Polyclonal and monoclonal antibodies were raised against mature oocyte extracts. The binding sites of these rabbit and hybridoma antibodies with the different yolk protein components were identified with a combination of WESTERN blotting, ELISA, immunofluorescence and immunogold staining. All these techniques demonstrated materials immunologically similar to vitellins in the hemolymph and in the glandular cells of the digestive gland. The data suggest that, for its vitellogenesis, the garden-snail utilizes a heterosynthetic mechanism similar to that known in oviparous animals. The vitellogenins would be produced by the digestive gland.
Barre
P
P
Laboratoire de Zoologie Embryologie UA CNRS 687, Faculté des Sciences et des Techniques, Universite de Besançon, France.
Bride
M
M
Beliard
R
R
Petracca
B
B
D000818:Animals; D000911:Antibodies, Monoclonal; D004064:Digestive System / Q000737:chemistry; D004527:Egg Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D005455:Fluorescent Antibody Technique; D006372:Helix, Snails / Q000737:chemistry*; D006458:Hemolymph / Q000737:chemistry; D007150:Immunohistochemistry; D009865:Oocytes / Q000737:chemistry*; D011498:Protein Precursors / Q000032:analysis*; D014819:Vitellogenins / Q000032:analysis
D000911:Antibodies, Monoclonal; D004527:Egg Proteins; D011498:Protein Precursors; D014819:Vitellogenins