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Identification of the glycosylation pattern of meat proteins in tissues from bovine myelin
Authors:Theofanis Katsiferis  Horst Wiethölter
Affiliation:1. Department of Food Technology and Nutrition, Technological Educational Institution of Athens, 12 Agiou Spyridonos Street, 122 10 Egaleo, Athens, Greece;2. Department of Neurology, Bürgerhospital, Klinikum Stuttgart, Tunzhofer Strasse 14-16, 70191 Stuttgart, Germany
Abstract:A variant form of Creutzfeld–Jacob disease in humans is associated with the consumption of food contaminated with the bovine central neural system. This has focused attention on the need for procedures to detect tissues of the neural system in meat and meat products. A method was developed for the identification of myelin glycoproteins in bovine neural tissue. The glycosylated structures of glycoproteins in different protein mixtures from central nervous system (CNS) and peripheral nervous system (PNS) isolated from bovine myelin were identified by the specific lectin–glycoprotein reactions. Digoxigenin-labeled lectins bonded to the terminal glycoconjugate sequences of nine CNS glycoproteins ranging from 15 to 200 kDa and four PNS glycoproteins ranging from 22 to 105 kDa. Datura stramonium (DSA) recognized the epitope Galβ1–4GlcNAc by two CNS and three PNS glycoproteins. Maackia amurensis (MAA) recognized the epitope NeuAcα2–3Gal by four CNS and two PNS glycoproteins. The peanut Arachis hypogaea (PNA) reacted with the high molecular CNS glycoprotein (200 kDa) with the sequence Galβ1–3GalNAc. Galanthus nivalis (GNA) bonded to mannose subunits linked α1–3 and α1–6 by six CNS glycoproteins with molecular weights between 17 and 200 kDa. Four of these glycoproteins were recognized from monoclonal antibodies against the “HNK-1 epitope”.
Keywords:Immunoblotting  Bovine  Lectins  Nervous system  Glycoproteins
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