Hplc Purification and Monoclonal Antibody Western Immunoblotting of Wheat Proteins to Investigate Coeliac Disease

1987 ◽  
Vol 73 (s17) ◽  
pp. 16P-16P
Author(s):  
AR Freedman ◽  
Wieser Wieser ◽  
HJ Ellis ◽  
PJ Ciclitira
Keyword(s):  
Monoclonal Antibody ◽  
Coeliac Disease ◽  
Wheat Proteins ◽  
Western Immunoblotting ◽  
Hplc Purification

scholarly journals Gut endocrine cell population in coeliac disease estimated by immunocytochemistry using a monoclonal antibody to chromogranin.

Gut ◽  
1986 ◽  
Vol 27 (7) ◽  
pp. 838-843 ◽  
Author(s):  
R Pietroletti ◽  
A E Bishop ◽  
F Carlei ◽  
M Bonamico ◽  
R V Lloyd ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Coeliac Disease ◽  
Cell Population ◽  
Endocrine Cell

A Radioimmunoassay for α-and β-Gliadins

1983 ◽  
Vol 64 (6) ◽  
pp. 655-659 ◽  
Author(s):  
P. J. Ciclitira ◽  
E. S. Lennox
Keyword(s):  
Staphylococcus Aureus ◽  
Coeliac Disease ◽  
Wheat Flour ◽  
Cross Reactivity ◽  
Competitive Binding ◽  
Gluten Free ◽  
Wheat Proteins ◽  
Specific Radioimmunoassay ◽  
Special Value ◽  
Antigen Antibody

1. A rapid, sensitive specific radioimmunoassay for α- and β-gliadin has been developed using an antiserum raised in rabbits to A-gliadin, a component of α-gliadin. 2. The antigen used in the assay was α-gliadin labelled with 125I; antigen-antibody complexes were collected after adsorption to Staphylococcus aureus in suspension. 3. The sensitivity of the assay, as judged by competitive binding with unlabelled antigen, was 1 ng of α- or β-gliadin, which show complete cross-reaction with this antiserum. 4. Cross-reactivity to other wheat proteins was < 1% and no cross-reactivity to extracts of rye, barley or oats was observed. 5. This radioimmunoassay for α- and β-gliadin has been used to measure their amount in different varieties of wheat flour, several foods prepared from flour, e.g. bread, biscuits and products prepared as ‘gluten free’. The possibility of assaying for α-gliadin in prepared foods is of special value since α-, β-, γ- and ω-gliadin have been shown to exacerbate coeliac disease.

Monoclonal antibody-based competitive assay for the sensitive detection of coeliac disease toxic prolamins

2005 ◽  
Vol 551 (1-2) ◽  
pp. 105-114 ◽  
Author(s):  
M.C. Bermudo Redondo ◽  
P.B. Griffin ◽  
M. Garzon Ransanz ◽  
H.J. Ellis ◽  
P.J. Ciclitira ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Coeliac Disease ◽  
Sensitive Detection ◽  
Competitive Assay

scholarly journals Natural variants of α-gliadin peptides with wheat proteins with reduced toxicity in coeliac disease – CORRIGENDUM

2020 ◽  
Vol 124 (4) ◽  
pp. 480-480
Author(s):  
Nika Japelj ◽  
Tanja Suligoj ◽  
Wei Zhang ◽  
Beatriz Côrte-Real ◽  
Joachim Messing ◽  
...  
Keyword(s):  
Coeliac Disease ◽  
Wheat Proteins ◽  
Natural Variants ◽  
Gliadin Peptides ◽  
Reduced Toxicity

A web-like network of type vi collagen in human skin is revealed by immuno-electron microscopy

1988 ◽  
Vol 46 ◽  
pp. 382-383
Author(s):  
Douglas R. Keene ◽  
Robert W. Glanville ◽  
Eva Engvall
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibody ◽  
Human Skin ◽  
Basement Membranes ◽  
Primary Antibody ◽  
Fat Cells ◽  
Secondary Antibody ◽  
Type Vi Collagen ◽  
Dermal Matrix ◽  
Immuno Electron Microscopy

A mouse monoclonal antibody (5C6) prepared against human type VI collagen (1) has been used in this study to immunolocalize type VI collagen in human skin. The enbloc method used involves exposing whole tissue pieces to primary antibody and 5 nm gold conjugated secondary antibody before fixation, and has been described in detail elsewhere (2).Biopsies were taken from individuals ranging in age from neonate to 65 years old. By immuno-electron microscopy, type VI collagen is found to be distributed as a fine branching network closely associated with (but not attached to) banded collagen fibrils containing types I and III collagen (Fig. 1). It appears to enwrap fibers, to weave between individual fibrils within a fiber, and to span the distance separating fibers, creating a “web-like network” which entraps fibers within deep papillary and reticular dermal layers (Fig. 2). Relative to that in the dermal matrix, the concentration of type VI collagen is higher around endothelial basement membranes limiting the outer boundaries of nerves, capillaries, and fat cells (Fig. 3).

High-voltage electron microscopy of subretinal scar formation

1992 ◽  
Vol 50 (1) ◽  
pp. 486-487
Author(s):  
G.E. Korte ◽  
M. Marko ◽  
G. Hageman
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibody ◽  
Retinal Pigment Epithelium ◽  
Glial Cells ◽  
High Voltage ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Sodium Iodate ◽  
High Voltage Electron Microscopy ◽  
Voltage Electron

Sodium iodate iv. damages the retinal pigment epithelium (RPE) in rabbits. Where RPE does not regenerate (e.g., 1,2) Muller glial cells (MC) forma subretinal scar that replaces RPE. The MC response was studied by HVEM in 3D computer reconstructions of serial thick sections, made using the STEREC0N program (3), and the HVEM at the NYS Dept. of Health in Albany, NY. Tissue was processed for HVEM or immunofluorescence localization of a monoclonal antibody recognizing MG microvilli (4).

Identification of the pulmonary syndrome hantavirus by direct and colloidal gold immune Electron Microscopy

1994 ◽  
Vol 52 ◽  
pp. 274-275
Author(s):  
C. D. Humphrey ◽  
C.S. Goldsmith ◽  
L. Elliott ◽  
S.R. Zaki
Keyword(s):  
Electron Microscopy ◽  
United States ◽  
Monoclonal Antibody ◽  
Colloidal Gold ◽  
Phosphotungstic Acid ◽  
Uranyl Acetate ◽  
Hantavirus Pulmonary Syndrome ◽  
Deer Mice ◽  
Immune Electron Microscopy ◽  
Negative Stain

An outbreak of unexplained acute pulmonary syndrome with high fatality was recognized in the spring of 1993 in the southwestern United States. The cause of the illness was quickly identified serologically and genetically as a hantavirus and the disease was named hantavirus pulmonary syndrome (HPS). Recently, the virus was isolated from deer mice which had been trapped near the homes of HPS patients, and cultivated in Vero E6 cells. We identified the cultivated virus by negative-stain direct and colloidal gold immune electron microscopy (EM).Virus was extracted, clarified, and concentrated from unfixed and 0.25% glutaraldehyde fixed supernatant fluids of infected Vero E6 cells by a procedure described previously. Concentrated virus suspensions tested by direct EM were applied to glow-discharge treated formvar-carbon filmed grids, blotted, and stained with 0.5% uranyl acetate (UA) or with 2% phosphotungstic acid (PTA) pH 6.5. Virus suspensions for immune colloidal gold identification were adsorbed similarly to filmed grids but incubated for 1 hr on drops of 1:50 diluted monoclonal antibody to Prospect Hill virus nucleoprotein or with 1:50 diluted sera from HPS virus infected deer mice.

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