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d galactose/sambucus
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Isolation and characterization of a new d-galactose-binding lectin from Sambucus racemosa L.
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A new acidic lectin from red elder (Sambucus racemosa L.) bark has been isolated by affinity chromatography and gel filtration. Noteworthy, and in contrast to other Sambucus species, red elder bark lacks acidic non-toxic type 2 ribosome-inactivating proteins but has basic ribosome-inactivating
alpha-D-galactose-bearing glycoproteins on the surface of stimulated murine peritoneal macrophages. Biochemical and immunochemical characterization of purified glycoproteins.
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Two glycoproteins were isolated from lysates of thioglycollate-stimulated, murine peritoneal macrophages by affinity chromatography on immobilized Griffonia simplicifolia I lectin and by preparative SDS/PAGE. The glycoproteins were readily labeled on the surface of intact macrophages with 3H and
Transient occurrence of an ebulin-related D-galactose-lectin in shoots of Sambucus ebulus L.
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Young shoots of Sambucus ebulus L. contain a monomeric d-galactose binding lectin (SELlm), which disappears upon shoot development, and was previously undetected since it co-purifies with the non-toxic type 2 ribosome-inactivating protein ebulin l and the dimeric lectin SELld. Molecular cloning of
Differential sensitivity of D-galactose-binding lectins from fruits of dwarf elder (Sambucus ebulus L.) to a simulated gastric fluid.
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Some lectins from Sambucus spp. share amino acid sequences with the pollen Sam n1 allergen. The lectins ebulin f and SELfd from the early stages of growth were isolated and subjected to analysis by MALDI-TOF mass spectrometry, tryptic peptide fingerprinting, molecular characterization and pepsin
[A method of selective histochemical analysis of sialoglycoproteins using lectins from elder (Sambucus nigra L.)].
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Good potentialities in application of elderberry (Sambucus nigra L.) bark lectin for selective histochemical identification of sialylated glycoconjugates has been demonstrated using lectin-peroxidase technique. In order to omit this lectin binding to D-galactose and N-acetyl-D-galactosamine
Comparison of structural changes of cell surface carbohydrates in the eustachian tube epithelium of chinchillas infected with a Streptococcus pneumoniae neuraminidase-deficient mutant or its isogenic parent strain.
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Six different lectin probes were used to examine alterations of the cell surface carbohydrates in the chinchilla eustachian tube (ET) lumen subsequent to the intranasal (i.n.) challenge with the Streptococcus pneumoniae parent strain, D39, or its isogenic derivative, DeltaNA1, which is deficient in
Comparison of alteration of cell surface carbohydrates of the chinchilla tubotympanum and colonial opacity phenotype of Streptococcus pneumoniae during experimental pneumococcal otitis media with or without an antecedent influenza A virus infection.
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Experimental and clinical studies suggest that influenza A virus promotes Streptococcus pneumoniae-induced otitis media; however, the mechanism underlying this synergistic interaction has not been completely defined. In this study, glycoconjugate expression patterns were evaluated on the cell
Lectinhistochemical detection of terminal carbohydrate residues in the enteric myxozoan Enteromyxum leei parasitizing gilthead seabream Sparus aurata (Pisces: Teleostei): a study using light and transmission electron microscopy.
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The presence of terminal carbohydrate residues in Enteromyxum leei (Diamant, Lom et Dyková, 1994) Palenzuela, Redondo et Alvarez-Pellitero, 2002 stages in gilthead seabream intestines was studied at light microscopy (LM) and transmission electron microscopy (TEM) level using lectin histochemical
Detection of carbohydrate terminals in the enteric parasite Enteromyxum scophthalmi (Myxozoa) and possible interactions with its fish host Psetta maxima.
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The existence and localisation of carbohydrate terminals in Enteromyxum scophthalmi stages was investigated at light (LM) and transmission electron microscopes (TEM) using lectin histochemistry techniques, with the aim of contributing to elucidate the participation of carbohydrate-lectin
Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.
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A third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid),
Isolation and molecular characterization of two lectins from dwarf elder (Sambucus ebulus L.) blossoms related to the Sam n1 allergen.
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Sambucus species contain a number of lectins with and without antiribosomal activity. Here, we show that dwarf elder (Sambucus ebulus L.) blossoms express two D-galactose-binding lectins that were isolated and purified by affinity chromatography and gel filtration. These proteins, which we named
Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and a structurally related new homodimeric lectin in fruits of Sambucus ebulus L.
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Mature leaves of dwarf elder (Sambucus ebulus L.) contain the non-toxic type 2 ribosome-inactivating protein ebulin 1 (Girbés et al., 1993b, J. Biol. Chem. 268: 18195-18199). We have now found that the green fruits of dwarf elder contain both free and polymerized forms of ebulin (ebulin f) and a new
cDNA molecular cloning and seasonal accumulation of an ebulin l-related dimeric lectin of dwarf elder (Sambucus ebulus L) leaves.
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SELld is a dimeric D-galactose and mucin-binding lectin (apparent Mr 68000) which coexists with the non-toxic type 2 ribosome-inactivating protein (RIP) ebulin l in dwarf elder (Sambucus ebulus L.) leaves. To ascertain a potential structural correlation with ebulin l molecular cloning of a cDNA
Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.
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A novel type 2 ribosome-inactivating protein (RIP) that we named ebulin 1 has been isolated from leaves of Sambucus ebulus L. (Caprifoliaceae). In vitro ebulin 1 strongly inhibited protein synthesis by rabbit reticulocyte lysates, rat brain, and rat liver cell-free systems but did not affect in
Cell-surface sialoglycoconjugate structures in wild-type and mutant Crithidia fasciculata.
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The cell-surface expression of sialoglycoconjugate structures in wild-type Crithidia fasciculata and its TFR(R1) drug-resistant mutant was analyzed with the aid of an influenza C virus strain, lectin, enzymatic treatment, and flow cytofluorimetry analysis probed with fluorescein
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