Gliadin, sensitivity

V7. Visakorpi, J. K., Gliadin tolerance test its applicability to the determination of gliadin sensitivity in coeliac patients. Ann. Paediat. Fenniae 5, 67-73 (1959). 

This chapter has reviewed the application of ROA to studies of unfolded proteins, an area of much current interest central to fundamental protein science and also to practical problems in areas as diverse as medicine and food science. Because the many discrete structure-sensitive bands present in protein ROA spectra, the technique provides a fresh perspective on the structure and behavior of unfolded proteins, and of unfolded sequences in proteins such as A-gliadin and prions which contain distinct structured and unstructured domains. It also provides new insight into the complexity of order in molten globule and reduced protein states, and of the more mobile sequences in fully folded proteins such as /1-lactoglobulin. With the promise of commercial ROA instruments becoming available in the near future, ROA should find many applications in protein science. Since many gene sequences code for natively unfolded proteins in addition to those coding for proteins with well-defined tertiary folds, both of which are equally accessible to ROA studies, ROA should find wide application in structural proteomics. 

Sensitivity to the protein gliadin, present in gluten, results in coeliac disease. 

Henterich et al. [51] returned to the initial AbiPrism 7700/TaqMan system for the detection of gliadin in food samples, with a 30-fold gain in sensitivity... 

Marsh, M.N., Morgan, S., Ensari, A., Wardle, T., Lobley, R., Mills, C., Auricchio, S. 1995. In vivo activity of peptide 31 —43,44—55,56-68 of alfa-gliadin in gluten sensitive entherop-athy (GSE). Gastroenterology 108 A871. 

Schwertz E, Kahlenberg F, Sack U, Richter T, Stern M, Conrad K, et al. Serologic assay based on gliadin-related nonapeptides as a highly sensitive and specific diagnostic aid in celiac disease. Clin Chem 2004 50 2370-2375. 

The diagnostic efficiency of autoantibody determination was found to exceed that of gliadin antibodies [117, 118]. Autoantibody tests were based mainly on the determination of IgA immunoglobulins against endomysium, human umbilical cord, and tTG. These autoantibodies were highly sensitive and specific with values for both parameters exceeding 95% in most studies [118-121],... 

Gliadin Gliadin, a glycoprotein derived from gluten, is extracted from wheat and separated by capillary electrophoresis [34,35]. Gliadin is classified as co-5, co-1,2, a, and y- type based on its structure and electrophoretic mobility [36].The glycoprotein is water insoluble due to the presence of interpolypeptide disulfide bonds and hydrophobic interactions. A limitation on the use of gliadins is that patient sensitivity causes an autoimmune disorder called celiac disease. 

Gliadin. A protein that is found in wheat and some other grains, including oats, rye, barley, and millet. People with coeliac disease are sensitive to gliadin in the diet and produce antibodies to gliadin as well as autoantibodies to tissue transglutaminase. 

Synonyms gluten-sensitive enteropathy, nontropical sprue Definition hypersensitivity to gluten (and gliadin), resulting in loss of small bowel villi and malabsorption... 

RP-HPLC also rapidly became important and widely used. Early studies showed resolution of wheat and maize proteins by RP-HPLC to be equal or superior to that of other methods [7]. For example, gliadin was resolved into more than 50 peaks and shoulders in 50min on a Cig column at 60 C [53]. RP-HPLC is also more rapid, sensitive, and reproducible than SE-HPLC it gives good quantitation and recovery and it is suitable for both preparative and analytical separations. Proteins resolve primarily on the basis of differences in surface hydrophobicity therefore, RP-HPLC complements techniques such as gel electrophoresis based on size or charge [7,93,94],... 

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