Epiglycanin-immunoreactive glycoproteins in mouse fetal tissues and fetal cells in culture.
Fetal tissues from time-pregnant female A/J mice of 16- and 19-day pregnancies and from neonates 1 day after birth, as well as from fetal cells in culture, absorbed significant amounts of anti-epiglycanin antibody. Detergent-solubilized glycoproteins, with epiglycanin activity, from fetal tissues and cells were separated by polyacrylamide gel electrophoresis, and the protein bands electroblotted onto a nitrocellulose gel. After the antigens were labeled with rabbit anti-epiglycanin antiserum and [125I]epiglycanin, autoradiography revealed two major bands containing the antigenic determinant at Mr 90,000 and 82,000. Bands of similar molecular weights, but with no demonstrated immunologic cross-reactivity, were observed by fluorography, if intact cells prior to solubilization were labeled by galactose oxidase followed by sodium borotritiide. Immunoreactive epiglycanin activity could be destroyed by Pronase, endo-N-acetyl-alpha-D-galactosaminidase (Diplococcus pneumoniae), or periodate oxidation. Activity was enhanced with neuraminidase. The spleen, liver, or erythrocytes from adult A/J mice did not possess the antigen, but incubation of adult spleen or liver with neuraminidase (Vibrio cholerae) exposed the epitope.
D000818:Animals; D000954:Antigens, Surface / Q000032:analysis; D001345:Autoradiography; D002478:Cells, Cultured; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D005333:Fetus / Q000378:metabolism*; D006023:Glycoproteins / Q000032:analysis* / Q000276:immunology; D008562:Membrane Glycoproteins; D051379:Mice; D019158:N-Acetylneuraminic Acid; D009363:Neoplasm Proteins / Q000032:analysis*; D012794:Sialic Acids / Q000378:metabolism
D000954:Antigens, Surface; D000939:Epitopes; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D009363:Neoplasm Proteins; D012794:Sialic Acids; C016424:epiglycanin protein, mouse; D019158:N-Acetylneuraminic Acid