A B Czuppon

Learn More
In the present work, 500 and 50,000 porcine zonae pellucidae were solubilized using Lithium-3,5-diiodosalicylate. The zona antigens were purified by immunoaffinity chromatography (IAC) on immobilized antizona immunoglobulin G (IgG). The antizona-IgG was raised by immunization of female rabbits with 500 heat-solubilized porcine zonae. Four antigens could be(More)
The lack of a more detailed study of spermatozoal antigens lies partly in the difficulty of adequate purification procedures. In the present work a spermatozoal cell membrane antigen was isolated using lithium 3,5-diiodosalicylate as the solubilizing agent. Its apparent molecular weight is 40 500 by gel filtration chromatography and 35 000 by dodecyl(More)
Antigenic spermatozoal polypeptides were purified by immunoaffinity chromatography, using immobilized immunoglobulin G from a sterile woman. One of these peptides showed Asp as N-terminal amino acid and had a sequence of Asp-Pro-Trp-Trp-Cys-Phe-Asp-Lys-Phe-Glu. Following synthesis, the synthetic peptide was tested in immunoinhibition test for its ability to(More)
Four O-glycosidic oligosaccharides (I, II, III, IV) were purified from a human spermatozoal sialoglycoprotein antigen following quantitative beta-elimination and reduction of the linkage sugar by KHB4+. The four oligosaccharides showed a similar carbohydrate composition consisting of sialic acids, galactose, fucose, galactosamine and N-acetylgalactosamine,(More)
Porcine zona pellucida were solubilized by treatment with lithium 3,5-diiodosalicylate. Following further purification by phenol/water extraction, ethanol precipitation and high performance liquid chromatography a total of 11 fractions were obtained. Fractions in the molecular mass range, that were previously found to possess antigenic properties, were(More)