erythrina/carbohydrate

The cDNA of the Erythrina corallodendron lectin (ECorL) has been expressed in Escherichia coli. For this purpose, an NcoI site was inserted into the cDNA coding for the lectin precursor [Arango, R., Rozenblatt, S. & Sharon, N. (1990) FEBS Lett. 264, 109-112] immediately before the codon GTG

Lectins from Erythrina cristagalli (EGA) and Erythrina corallodendron (ECorA) are well-known to detect type 2 chain oligosaccharides (Gal beta 1-4GlcNAc). These carbohydrate moieties are the biosynthetic precursors of various ABH and Lewis blood group antigens and are therefore also related to

The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary

Alpha-D-Mannosidase (EC: 3.2.1.24), a glycoprotein with 8.6% carbohydrate was purified (26 fold purification) to homogeneity from Erythrina indica seeds, by gel filtration on Bio-Gel P-100 and affinity chromatography on Con-A CL Seralose. The enzyme had the molecular mass of 124 kDa and 127 kDa by

Erythrina cristagalli lectin (ECL) is a galactose-specific legume lectin. Although its biological function in the legume is unknown, ECL exhibits hemagglutinating activity in vitro and is mitogenic for T lymphocytes. In addition, it has been recently shown that ECL forms a novel conjugate when

Erythrina corallodendron lectin (ECorL) exhibits an exquisitely structured oligosaccharide chain. Interestingly, the bacterially expressed, nonglycosylated counterpart, rECorL, possesses an essentially identical carbohydrate specificity and agglutinating activity as the glycosylated lectin, thus

An examination of fluorescein-labelled Erythrina cristigalli lectin (FITC-ECL) staining on feline mononuclear cells (MNC) using fluorescent microscopy and a novel sugar titration competition assay revealed that monocytes (MO) were stained brighter by FITC-ECL than were lymphocytes (LYM). When MNC

Lectins are carbohydrate-binding proteins, which occur ubiquitously in nature and are abundant in all living organisms from bacteria to mammals. They have several biological functions among which cell adhesion is well known and characterized. Based on the characterization of the glycome of human

Previous studies on the carbohydrate specificities of Erythrina cristagalli lectin (ECL) were mainly limited to analyzing the binding of oligo-antennary Galbeta1-->4GlcNAc (II). In this report, a wider range of recognition factors of ECL toward known mammalian ligands and glycans were examined by

High-resolution X-ray crystallography of the complex of the Gal/GalNAc-specific Erythrina corallodendron lectin with lactose identified the amino acid side chains that form contacts with the galactose moiety of the disaccharide. The contribution of these amino acids to the binding of different

A lectin was purified from seeds of Erythrina velutina forma aurantiaca by affinity chromatography on cross-linked guar gum. The lectin is a potent agglutinin for human (minimal concentration of protein able to cause visible agglutination of a 2% erythrocyte suspension varying from 1 to 4

The equilibrium unfolding of ElysL, a homodimeric legume lectin, was studied using different denaturing agents such as guanidinium chloride (GdnHCl), temperature and pH. Simultaneously, changes in the secondary as well as tertiary structure of lectin were followed by CD spectroscopy examination in

BACKGROUND Erythrina corallodendron lectin (ECorL) is one of the potent applied lectins. In previous studies, the carbohydrate specificities of this lectin were limited to monosaccharides, simple oligosaccharides and several clusters. However, the polyvalent factor has not been

A lectin was isolated from the saline extract of Erythrina speciosa seeds by affinity chromatography on lactose-Sepharose. The lectin content was about 265 mg/100g dry flour. E. speciosa seed lectin (EspecL) agglutinated all human RBC types, showing no human blood group specificity; however a slight

The structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type