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moluccella/lectin
הקישור נשמר בלוח
10 תוצאות
Characterization of the specificity of binding of Moluccella laevis lectin to glycosphingolipids.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The specificity of Moluccella laevis lectin was investigated by analysing its binding to glycosphingolipids separated on thin-layer chromatograms or adsorbed on microtitre wells. The binding activity of the lectin was highest for glycosphingolipids with terminal alpha-linked N-acetylgalactosamine,
Moluccella laevis lectin, a marker for cellular differentiation programs in mouse gut epithelium.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
We have assembled a system for testing the hypothesis that changes in glycoconjugate production represent markers for defining developmental, spatial, and environmental influences on the proliferation and differentiation programs of various mouse gut epithelial cell lineages. Multilabel
Immunochemical studies on the combining site of the A + N blood type specific Moluccella laevis lectin.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The specificity of the anti A+N lectin of Moluccella laevis (MLL) was examined by hemagglutination experiments with enzyme-modified human erythrocytes and by inhibition of hemagglutination. In addition, binding to various glycoproteins and inhibition by different sugars and glycoproteins were
Isolation, by affinity chromatography and gel filtration in 8 M-urea, of an active subunit from the anti-(blood-group A+N)-specific lectin of Moluccella laevis.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The lectin from Moluccella laevis seeds agglutinates specifically blood-type-A and -N erythrocytes, and both activities are inhibited by micromolar concentrations of N-acetyl-D-galactosamine. The lectin consists of three subunits: a 67 kDa heterodimer, made up of two S-S-linked polypeptides of 28
Vicia villosa B4 lectin is the second anti-Tn lectin shown to react better with blood group N than M antigen.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Earlier studies showed that Moluccella laevis lectin, which has anti-Tn specificity, reacts more strongly with native or desialylated blood group N glycophorin A than with the respective glycophorins of blood group M. We now present results indicating that Vicia villosa B4 anti-Tn lectin, which does
Use of O-glycosylation-defective human lymphoid cell lines and flow cytometry to delineate the specificity of Moluccella laevis lectin and monoclonal antibody 5F4 for the Tn antigen (GalNAc alpha 1-O-Ser/Thr).
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The Tn antigen (GalNAc alpha 1-O-Ser/Thr) is a disease-related O-linked (mucin-type) carbohydrate neoantigen which is expressed in idiopathic Tn syndrome, AIDS, T-cell lymphoma and in many carcinomas. In the present study, we took advantage of a Tn antigen expressing T-lymphocyte clone derived from
Dramatic saccharide-mediated protection of chaotropic-induced deactivation of concanavalin A.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
This work provides evidence of a physical instance in which some proteins that are usually inactivated under strong chaotropic conditions may become fully resistant through the occupancy of their binding sites with suitable ligands. In this regard, we found that Moluccella laevis lectin remains
Blood group MN-dependent difference in degree of galactosylation of O-glycans of glycophorin A is restricted to the GalNAc residues located on amino acid residues 2-4 of the glycophorin polypeptide chain.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Glycophorin A (GPA) of human erythrocytes contains a minor number of unsubstituted GalNAc residues (Tn receptors) which are recognized by Moluccella laevis lectin (MLL). The lectin reacts better with blood group N- than M-type of GPA which suggests a higher number of Tn receptors in GPA-N than in
Further characterization of some heterophile agglutinins reacting with alkali-labile carbohydrate chains of human erythrocyte glycoproteins.
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The nature of the receptor sites for several agglutinins is characterized by hemagglutination inhibition assays. The inhibitory activity of human erythrocytes glycoproteins, from which sialic acid, sialic acid and galactose or alkali-labile oligosaccharides have been removed, is compared to the
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