Search results for "Concanavalin A"

Effects of succinylation on thermal induced amyloid formation in Concanavalin A.

2007

We have recently shown that upon slight thermal destabilization the legume lectin Concanavalin A may undergo two different aggregation processes, leading, respectively, to amyloid fibrils at high pH and amorphous aggregates at low pH. Here we present an experimental study on the amyloid aggregation of Succinyl Concanavalin A, which is a dimeric active variant of Concanavalin. The results show that, as for the native protein, the fibrillation process appears to be favoured by alkaline pH, far from the isoelectric point of the protein. Moreover, it strongly depends on temperature and requires large conformational changes both at secondary and tertiary structure level. With respect to the nati…

Concanavalin A toxicity on Neuroblastoma LAN5 cell cultures

2007

CONCANAVALIN A AGGREGATION AND TOXICITY ON NEUROBLASTOMA LAN5 CELL CULTURES

2009

Molecular mechanisms in thermally induced amyloid formation of Concanavalin A

2008

Amyloid Fibrils Formation in Concanavalin A studied by Dynamic Light Scattering and Fluorescence techniques

2007

Chitin synthetase activity in Candida albicans: subcellular distribution in yeast cells and protoplasts

1991

Chitin synthetase activity was detected in a partly zymogenic form in cell-free homogenates obtained from C. albicans yeast cells and protoplasts of the same type of cells. By isopycnic centrifugation on sucrose gradients of the cell-free homogenates two fractions with chitin synthetase activity were obtained: one was associated with the plasma membrane (labelled with [ 3 H]concanavalin A (con A) and buoyant density 1·195 g ml −1 ) in a partly active state, and the second was in the cytoplasm, where the enzyme was in a particulate fully zymogenic form, lacking affinity to con A. The buoyant density of the enzyme found in this location depended on the method of cell breakage. Lysis of partly…

A D-mannose-specific lectin from Gerardia savaglia that inhibits nucleocytoplasmic transport of mRNA.

1987

A new lectin has been isolated from the coral Gerardia savaglia by affinity chromatography, using locust gum as an absorbent, and D-mannose as eluant. Final purification was achieved by Bio-Gel P300 gel filtration. The agglutinin is a protein composed of two polypeptide chains with a Mr of 14800; the two subunits are not linked by disulfide bond(s). The isoelectric point is 4.8, the amino acid composition is rich in the acidic amino acids aspartic acid and glutamic acid. The absorption maximum for the protein was at 276 nm; with a molar absorption coefficient of 1.27 X 10(5) M-1 cm-1. The lectin precipitated erythrocytes from humans (A, B and O), sheep, rabbit and carp with a titer between …

Chitosomes lack concanavalin-A-binding sites

1985

Whether intact or dissociated with digitonin, chitosomes isolated from the fungusMucor rouxii lack the ability to bind concanavalin A. The absence of external or internal concanavalin A-binding sites distinguishes the chitosome membrane no only from plasma membrane but also from membranes of other organelles (endoplasmic reticulum, mitochondrion, vacuole). This differential binding ability was used to partially separate chitosomal chitin synthetase from major membranes in a crude cell-free extract ofM. rouxii.

Dynamic evaluation of aggregation and agglutination of red blood cells.

1984

Viscoelastic evaluation of aggregation and agglutination of red blood cells was attempted. A concentric double cylinder viscoelastometer was used for determining the dynamic rigidity modulus and loss modulus of blood sample. The dynamic rigidity modulus of horse blood were measured over a wide range of hematocrit. The relation between the viscoelastic behavior and the erythrocyte sedimentation was examined. The change in the amount of surface charge of enzyme treated red blood cells was qualitatively estimated from the measurements of dynamic viscoelasticity of red blood cells suspension with added poly-L-lysine. The dynamic rigidity modulus of red blood cells agglutinated by adding lectin …

Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils

2020

The formation of amyloid structures has traditionally been related to human neurodegenerative pathologies and, in recent years, the interest in these highly stable nanostructures was extended to biomaterial sciences. A common method to monitor amyloid growth is the analysis of Thioflavin T fluorescence. The use of this highly selective dye, diffused worldwide, allows mechanistic studies of supramolecular assemblies also giving back important insight on the structure of these aggregates. Here we present experimental evidence of self-quenching effect of Thioflavin T in presence of amyloid fibrils. A significant reduction of fluorescence lifetime of this dye which is not related to the propert…