title: Conformational epitopes on interstitial collagens.
abstract: The antigenic response to the helical domain of collagens is normally very low, with the nature of the epitopes recognized by antibodies being dependent on the species of origin. Thus, in certain species, for example rabbit, sequential determinants on single alpha-chains are found, whereas in other species such as mouse, conformational epitopes are predominant. A variety of techniques for identification of epitopes, including rotary shadowing, examination of specific fragments and chemical modification reactions are discussed. The application of these techniques is illustrated using a range of monoclonal antibodies to interstitial collagens. These antibodies show that epitopes are distributed over the length of the collagen molecule.
authors.affiliation: CSIRO, Division of Biomolecular Engineering, Parkvile, Victoria, Australia.
authors.forename: V
authors.initials: V
authors.lastname: Glattauer
authors.forename: J A
authors.initials: JA
authors.lastname: Ramshaw
authors.forename: T A
authors.initials: TA
authors.lastname: Tebb
authors.forename: J A
authors.initials: JA
authors.lastname: Werkmeister
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology; D000937:Antigen-Antibody Reactions; D003094:Collagen / Q000276:immunology* / Q000648:ultrastructure; D000939:Epitopes / Q000276:immunology; D008854:Microscopy, Electron; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013045:Species Specificity
chemical_list: D000911:Antibodies, Monoclonal; D000939:Epitopes; D003094:Collagen