Specificities of Monoclonal Antibodies to Domain I of α-Gliadins

References

• Van de Kamer J H, Weijers H A, Dicke WK. Coeliac disease. IV. An investigation into the injurious constituents of wheat in connection with their action on patients with coeliac disease. Acta Paediatr 1953; 42: 223–31
   PubMedGoogle Scholar
• Hekkens W TJ M, Haex A JC, Willighagen R GJ (1970) Some aspects of gliadin fractionation and testing by a histochemical method. Coeliac disease. Proceedings of the International Coeliac Symposium. 1969, CC Booth, RH Dowling. Churchill Livingstone, Edinburgh, 11–9
   Google Scholar
• Jos J, Charbonier L, Mosse J, Olives J P, de Tand M-F, Rey J. The toxic fraction of gliadin digests in coeliac disease. Isolation by chromatography on Biogel P-10. Clin Chim Acta 1982; 119: 263–74
   PubMed Web of Science ®Google Scholar
• Howdle P D, Ciclitira P J, Simpson F G, Losowsky MS. Are all gliadins toxic in coeliac disease? An in vitro study of α, β, γ and ω gliadins. Scand J Gastroenterol 1984; 19: 41–7
   PubMed Web of Science ®Google Scholar
• Ciclitira P J, Evans D J, Fagg N LK, Lennox E S, Dowling RH. Clinical testing of gliadin fractions in coeliac patients. Clin Sci 1984; 66: 357–64
   PubMed Web of Science ®Google Scholar
• Wieser H, Springer G, Belitz H-D, Ashkenazi A, Idar D. Toxicity of different wheat gliadins in coeliac disease. Z Leb-ensm Unters Forsch 1982; 175: 321–6
   PubMedGoogle Scholar
• Wieser H, Belitz H-D, Ashkenazi A, Idar D. Isolation of coeliac active peptide fractions from gliadin. Z Lebensm Unters Forsch 1983; 176: 85–94
   PubMedGoogle Scholar
• Wieser H, Belitz H-D, Ashkenazi A. Amino-acid sequence of the coeliac active gliadin peptide B3142. Z Lebensm Unters Forsch 1984; 179: 371–6
   PubMedGoogle Scholar
• de Ritis G, Auricchio S, Jones H W, Lew EJ-L, Bernardin J E, Kasarda DD. In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease. Gastroenterology 1988; 94: 41–9
   PubMed Web of Science ®Google Scholar
• Jos J, de Tand M-F, Arnaud-Battandier F, Boissel J P, Popineau Y, Wajcman H. Separation of pure toxic peptides from a β-gliadin subfraction using high-performance liquid chromatography. Clin Chim Acta 1983; 134: 189–98
   PubMed Web of Science ®Google Scholar
• Devery J M, Bender V, Penttila I, Skerritt JH. Identification of reactive synthetic gliadin peptides specific for coeliac disease. Int Arch All Appl Immunol 1991; 95: 356–62
   PubMedGoogle Scholar
• Wieser H, Belitz H-D. Coeliac active peptides from gliadin:large scale preparation and characterization. Z Lebensm Unters Forsch 1992; 194: 229–34
   PubMedGoogle Scholar
• Patey A L, Evans DJ. Large scale preparation of gliadin proteins. J Sci Food Agric 1973; 24: 1229–33
   PubMed Web of Science ®Google Scholar
• Ciclitira P J, Ellis H J, Evans D J, Lennox ES. A radioimmunoassay for wheat gliadin to assess the suitability of gluten-free foods for patients with coeliac disease. Clin Exp Immunol 1985; 59: 703–8
   PubMedGoogle Scholar
• Frazer A C, Fletcher R F, Ross C AC, Shaw B, Sammons H G, Schnbeider R. Gluten induced enteropathy:the effect of partially digested gluten. Lancet 1959; 2: 252–5
   PubMed Web of Science ®Google Scholar
• Lowry O H, Rosebrough N J, Farr A L, Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem 1951; 193: 265–75
   PubMed Web of Science ®Google Scholar
• Payne P I, Cornfield KG. Subunit composition of wheat glutenin proteins, isolated by gel filtration in a dissociating medium. Planta 1979; 145: 83–8
   PubMed Web of Science ®Google Scholar
• Kasarda D D, Okita T W, Bernadin J E, et al. Nucleic acid (cDNA) and amino acid sequences of ir-type gliadins from wheat (Triticum aestiuum). Proc Natl Acad Sci 1984; 81: 4712–6
   PubMed Web of Science ®Google Scholar
• Wieser H, Belitz H-D, Idar D, Ashkenazi A. Coeliac activity of the gliadin peptides CT1 and CT2. Z Lebensm Unters Forsch 1986; 182: 115–7
   PubMedGoogle Scholar
• Ellis H J, Freedman A R, Ciclitira PJ. The production and characterisation of monoclonal antibodies to wheat gliadin peptides. J Immunol Method 1989; 120: 17–22
   PubMed Web of Science ®Google Scholar
• Kearney J F, Radbruch A, Liesegang B, Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody secreting hybrid cells lines. J Immunol 1979; 123: 1548–50
   PubMed Web of Science ®Google Scholar
• Galfre G, Milstein C. Preparation of monoclonal antibodies. Strategies and procedures. Methods Enzymol 1981; 73: 3–46
   PubMedGoogle Scholar
• Freedman A R, Galfre G, Gal E, Ellis H J, Ciclitira PJ. Detection of wheat gliadin contamination of gluten-free foods by monoclonal antibody dot immunobinding assay. Clin Chim Acta 1987; 166: 323–8
   PubMed Web of Science ®Google Scholar
• Freedman A R, Galfre G, Gal E, Ellis H J, Ciclitira PJ. Western immunoblotting of cereal proteins. Int Arch Allergy Appl Immunol 1988; 85: 346–50
   PubMedGoogle Scholar
• Bietz J A, Wall JS. Identity of high molecular weight gliadin and ethanol-soluble glutenin subunits of wheat:relation to gluten structure. Cereal Chem 1980; 57: 415–21
   Google Scholar
• Shewry P R, Miflin G J, Lew EJ-L, Kasarda DD. The preparation and characterisation of an aggregated gliadin fraction from wheat. J Exp Botany 1983; 34: 1403–10
   Web of Science ®Google Scholar
• Auricchio S, de Ritis G, Maiuri L, et al. A-gliadin related synthetic peptides:damaging effects on in vitro cultured atrophic celiac intestinal mucosa and developing fetal rat intestine. Gastroenterology 1991; 100: A194
   Google Scholar
• Tatham A S, Marsh M N, Wieser H, Shewry PR. Conformational studies of peptides corresponding to the coeliac-activating regions of wheat α-gliadin. Biochem J 1990; 270: 313–8
   PubMed Web of Science ®Google Scholar
• Tatham A S, Drake A F, Shewry PR. Conformational studies of a synthetic peptide corresponding to the repeat motif of C-hordein. Biochem J 1989; 259: 471–6
   PubMedGoogle Scholar