title: Investigation of gliadin binding to different selected proteins using a biotin-streptavidin system.
abstract: Using a biotin streptavidin system 12 out of 19 different test proteins were found to bind to gliadin, with casein, fibrinogen, and fibronectin showing the strongest association. Binding was demonstrable using different gliadin subfractions and enzymatic digests. There was no consistent effect of several carbohydrates on binding. Binding of most proteins to gliadin was diminished slightly by removal of Ca2+ and strongly by dioxane, ethylene glycol, Triton X-100, and Tween 20. The results suggest a non-selective association between gliadin and the proteins investigated, mainly due to hydrophobic interactions, which might be of significance in intestinal pathobiochemistry, e.g. disease.
authors.affiliation: Institute of Pathological Biochemistry, Medical Department of the University, Leipzig, Germany.
authors.forename: A A
authors.initials: AA
authors.lastname: Osman
authors.forename: I
authors.initials: I
authors.lastname: Braunersreuther
authors.forename: T
authors.initials: T
authors.lastname: Mothes
mesh_terms: D000818:Animals; D001426:Bacterial Proteins; D001710:Biotin; D002364:Caseins / Q000378:metabolism; D002417:Cattle; D005340:Fibrinogen / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D005903:Gliadin / Q000378:metabolism*; D006801:Humans; D009077:Mucins / Q000378:metabolism; D011485:Protein Binding; D019809:Streptavidin
chemical_list: D001426:Bacterial Proteins; D002364:Caseins; D005353:Fibronectins; D009077:Mucins; D001710:Biotin; D005340:Fibrinogen; D005903:Gliadin; D019809:Streptavidin