Association of Immunostaining of Galectin-3 and Sambucus nigra Agglutinin with Invasion, Metastasis and Poor Progression of Gallbladder Adenocarcinoma

2012 ◽  
Author(s):  
Le-ping Yang ◽  
Song Jiang ◽  
Jie-qiong Liu ◽  
Xiong-ying Miao ◽  
Zhu-lin Yang
Keyword(s):  
Sambucus Nigra ◽  
Sambucus Nigra Agglutinin ◽  
Galectin 3 ◽  
Gallbladder Adenocarcinoma

Effects of Sialic Acid Substitutions on Recognition by Sambucus nigra Agglutinin and Maackia amurensis Hemagglutinin

2002 ◽  
Vol 303 (1) ◽  
pp. 98-104 ◽  
Author(s):  
Els C.M. Brinkman-Van der Linden ◽  
Justin L. Sonnenburg ◽  
Ajit Varki
Keyword(s):  
Sialic Acid ◽  
Sambucus Nigra ◽  
Maackia Amurensis ◽  
Sambucus Nigra Agglutinin

scholarly journals A sub-population of keratan sulphates derived from bovine articular cartilage is capped with α(2–6)-linked N-acetylneuraminic acid residues. Affinity chromatography using immobilized Sambucus nigra lectin and characterization using 1H n.m.r. spectroscopy

1992 ◽  
Vol 286 (1) ◽  
pp. 231-234 ◽  
Author(s):  
G H Tai ◽  
H G Morris ◽  
G M Brown ◽  
T N Huckerby ◽  
I A Nieduszynski
Keyword(s):  
Affinity Chromatography ◽  
Gel Permeation Chromatography ◽  
Similar Proportion ◽  
Lectin Affinity Chromatography ◽  
Sambucus Nigra ◽  
Keratan Sulphate ◽  
Bovine Articular Cartilage ◽  
Acetylneuraminic Acid ◽  
Sambucus Nigra Agglutinin ◽  
Femoral Head Cartilage

Alkaline borohydride-reduced keratan sulphate (KS) chains derived from bovine femoral head cartilage were fractionated by lectin affinity chromatography with Sambucus nigra agglutinin (SNA) into binding and non-binding populations. Analysis of the SNA-binding and non-binding KS chains using 600 MHz 1H n.m.r. spectroscopy showed that the former population contained alpha(2-6)-N-acetylneuraminic acid residues and the latter contained primarily alpha(2-3)-N-acetylneuraminic acid residues as chain terminators. Both populations contained a similar proportion of alpha(2-3)-N-acetylneuraminic acid residues within their protein-linkage regions, and similar sulphation and fucosylation levels. Analysis of these two fractions by gel-permeation chromatography (g.p.c.) on a TSK-30 XL column showed them to have the same size distributions. It was concluded from the n.m.r. spectra and g.p.c. data that the populations differed primarily in the mode of linkage of the chain-terminating sialic acids.

scholarly journals Purification and partial characterization of a novel lectin from elder (Sambucus nigra L.) fruit

1991 ◽  
Vol 278 (3) ◽  
pp. 667-671 ◽  
Author(s):  
L Mach ◽  
W Scherf ◽  
M Ammann ◽  
J Poetsch ◽  
W Bertsch ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Carbohydrate Specificity ◽  
Sambucus Nigra ◽  
Acid Glycoprotein ◽  
High Affinity ◽  
Sambucus Nigra Agglutinin ◽  
Sds Page ◽  
Molecular Masses

A previously unknown haemagglutinin, named Sambucus nigra agglutinin-III (SNA-III), has been purified from the fruit of the elder (Sambucus nigra). Whereas elder bark agglutinin I (SNA-I) is highly specific for terminal alpha 2,6-linked sialic acid residues, SNA-III displays a high affinity for oligosaccharides containing exposed N-acetylgalactosamine and galactose residues. Different N-terminal sequences and the amino acid composition distinguish the fruit lectin from elder bark agglutinin II (SNA-II), which shows a similar carbohydrate specificity. The 40-fold higher affinity of SNA-III for asialofetuin than for human asialo-alpha 1-acid glycoprotein and human asialotransferrin respectively suggests a preference for O-linked glycans. SNA-III occurs mainly as a monomeric glycoprotein, but tends to form di- and oligo-meric aggregates. This aggregation seems to mediate the multivalent interaction, leading to agglutination. SDS/PAGE revealed two major polypeptides with apparent molecular masses of 32 and 33 kDa respectively. This heterogeneity is probably a result of proteolysis in the C-terminal region. Binding to concanavalin A and susceptibility to peptide: N-glycosidase F indicated the presence of N-glycosidically linked oligosaccharides.

scholarly journals Carbohydrate characterization of purified thyroxine-binding globulin by lectin blot and isoelectric focusing

2003 ◽  
Vol 22 (4) ◽  
pp. 319-323 ◽  
Author(s):  
Ivana Petrovic ◽  
Svetlana Savin-Zegarac ◽  
Ivona Baricevic ◽  
Dubravka Cvejic
Keyword(s):  
Sialic Acid ◽  
Isoelectric Focusing ◽  
Blot Analysis ◽  
Wheat Germ ◽  
Sambucus Nigra ◽  
Thyroxine Binding Globulin ◽  
Sambucus Nigra Agglutinin ◽  
Lectin Blot ◽  
Wheat Germ Lectin

The structure of carbohydrate moiety of purified thyroxine-binding globulin (TBG) was examined by lectin blot and isoelectric focusing (IEF). In lectin blot, TBG reacted positively with the following lectins: Sambucus nigra agglutinin (SNA I), Ricinus commuais agglutinin (RCA I), wheat germ lectin (WGA), phytoheamagglutinin (PHA) and pea lectin (PSA). The obtained results indicate that purified TBG contains N-linked oligosaccharide chains consisting of mannose, galactose, N-acetylglucosamine and sialic acid. Isoelectric focusing of TBG at pl 4.2-4.6 revealed three bands, which confirmed that isolated TBG had retained its structure with?out desialylation. Lectin blot analysis and IEF can be considered to be useful tools in the study of TBG glycosylation.

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