Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.2.2.10 (PNL)
 341 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monospecific antibodies directed to a Thomsen-Friedenreich antigen (T-antigen) were obtained using artificial antigen. T-antigen immunodominant alpha-disaccharide Galbeta (1----3) GalNAc alpha 1-(T alpha) and its beta-anomer Gal beta (1----3) GalNAc beta 1-(T beta) were bound to bovine serum albumin (BSA) and cytochrome C (CCC) through a spacer (sp = -O(CH2)3NHCO (CH2)4CO-) by the azide method to give neoglycoproteins T alpha-sp-BSA, T alpha-sp-CCC and T beta-sp-BSA. Anti-T alpha antiserum was obtained by immunization of rabbits with T alpha-sp-BSA and then purified by sequential affinity chromatography on BSA-Sepharose and T alpha-sp-BSA-Sepharose to yield monospecific anti-T IgG antibodies. As elucidated by ELISA method, binding T alpha-sp-BSA to the antibodies was inhibited by T alpha-sp-CCC, T alpha-sp-OEt, asialofetuin, T alpha-OBzl, the activity of the inhibitors decreasing in the above order. Methyl beta-galactopyranoside, benzyl 2-acetamido-2-deoxy-alpha-D-galactopyranoside, disaccharide Gal beta (1----3) GalNAc and H-sp-BSA were inactive. The inhibitory analysis suggests that both disaccharide moiety T alpha- and a definite part of the spacer are important for the binding and that T alpha-OCH2 seems to be the minimal recognized structure. In immunoprecipitation tests the antibodies react with T alpha-sp-BSA but not with T beta-sp-BSA, whereas peanut (Arachis hypogaea) lectin (PNL) precipitated both T alpha- and T beta-sp-BSA. These data suggest the significance of the alpha-galactosaminide bond for the antibody recognition. Desialylated human erithrocites (natural T-antigen) were effectively agglutinated with the antibodies. Murine cortical thymocytes (obtained by agglutination-sedimentation method using PNL) were agglutinated with the antibodies only partially (67%), while these cells as well as the cells unaffected by the antibodies were completely agglutinated with PNL. These results indicate to different contents of glycoproteins (T alpha) and glycolipids (T beta) oligosaccharide determinants on the surface of cortical thymocytes species.
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PMID:[Monospecific antibodies against synthetic T-antigen. Characteristics of their specificity and use in the identification of T-antigenic determinants on the cell surface]. 241 65

Histochemical study by traditional staining methods (AB, PAS, HID) and by the use of five peroxidase-labelled lectins (ConA, WGL, WPL, SBL, PNL) were carried out to characterize glycoconjugates in the secretory cells of the nasal mucosa of the Lacertid lizard Podarcis sicula campestris De Betta. The mucus covering the nasal epithelium is produced by the supporting cells and the Bowman glands in the olfactory area, and by typical goblet cells and, probably, a second type of secretory cell, in the non-sensory area. Neutral glycoconjugates containing N-acetyl-D-glucosamine and terminal N-acetyl-D-galactosamine, D-mannose and D-glucose residues were present in the secretory product of the Bowman glands. L-fucose and D-galactose were absent. In the supporting cells the secretory product consisted mainly of sulfated glycoproteins containing D-galactose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, D-mannose, D-glucose, but not L-fucose. Glycoconjugates containing terminal sialic acid and penultimate D-galactose were present in typical goblet cells as was N-acetyl-D-glucosamine.
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PMID:Lectin histochemistry of secretory cell glycoconjugates in the nasal mucosa of Podarcis sicula campestris De Betta (Reptilia, Lacertidae). 281 23

We investigated the structure of glycoconjugates contained within the secretory end-pieces and ductal segments in the rabbit submandibular and sublingual glands. Glycosidic sequences were examined by means of enzymatic degradation with specific glycosidases (sialidase, alpha-fucosidase, beta-galactosidase, alpha-mannosidase) followed by lectin binding with PNL-HRP, WPL-HRP, WGL-HRP, SBL-HRP, Con A-HRP. It was found that this procedure represents a valid tool for studying carbohydrates, in so far as their characterization and localization were based only on colour reactions. In particular, this research showed that sialic acid was present in the terminal dimers sialic acid-beta-galactose and sialic acid-N-acetyl-D-galactosamine within the submandibular gland, whereas in the sublingual gland it was only present as the sequence sialic acid-beta-galactose. Conversely, fucose had as the subterminal sugar N-acetyl-D-glucosamine in both glands. Also, elucidations about structural sequences concerning other non-terminal sugars were obtained.
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PMID:Visualization of carbohydrate chains in rabbit salivary glands by means of enzymatic degradation and plant lectins. 314 37

The ability of prenatal cerebral tissue to bind different lectins was analyzed using cryostat sections of mouse brains. It was shown that the immature cells within the embryonic cell layers possess receptors for different lectins in varying amounts. Of all lectins tested, only PNL, RCL and LPL were bound on the outer cell membranes to a considerable degree. Although the labeling patterns of PNL and RCL are similar, the latter is additionally well detectable on the wall of cerebral blood vessels. Cells of the ventricular layer are moderately labeled by PNL, which recognizes beta-D-galactosyl (1-3)-N-acetyl-D-galactosamine, but heavily labeled by LPL which binds to terminal sialic acid residues. Cells of the intermediate layer, on the other hand, are heavily stained PNL and only faintly by LPL. Hence it is suggested that the process of migration might be correlated to the removal of terminal sialic acid moieties from cell surface glycoconjugates, resulting in an exposure of the penultimate galactosyl residues.
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PMID:Varying expressions of lectin receptors within embryonic cell layers of murine cerebral cortex. 719 28

Mucous cells and enteroendocrine cells of the pyloric region of the ruin lizard (Podarcis sicula campestris De Betta) have been examined by lectin histochemical and immunohistochemical methods. Binding to five plant lectins (Canavalia ensiformis, Con A; Triticum vulgare, wheat germ, WGL; Lotus tetragonolobus, winged pea, WPL; Glycine max, soybean, SBL; Arachis hypogaea, peanut, PNL) was performed to characterize glycoconjugates in the secretory products of superficial and glandular mucous cells. Lectin histochemistry revealed the presence of N-acetyl-D-galactosamine, D-galactose and N-acetyl-D-glucosamine in the pyloric superficial cells. Mucous glandular cells mainly contained neutral glycoproteins with terminal residues of galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine. These cells did not react with Con A after periodate oxidation-sodium borohydride reduction (Paradoxical Con A staining). In the pyloric glands three different types of endocrine cells were identified immunohistochemically: gastrin-, serotonin- and somatostatin-immunoreactive cells; VIP-, bombesin- or cholecystokinin-immunoreactive cells have not been found in the pyloric mucosa.
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PMID:Immunohistochemical investigations on the pyloric glands of the ruin lizard (Podarcis sicula campestris de Betta). 791 80