Structural studies of human basement-membrane collagen with the use of a monoclonal antibody.
A monoclonal antibody monospecific for human type IV collagen was used as a structural probe to examine aspects of the macromolecular organization of basement-membrane collagen. Electron-microscopic observation of rotary-shadowed antigen-antibody complexes demonstrated a unique binding site for the antibody 55 +/- 6 nm distant from the 7S cross-linking region of tetrameric type IV collagen. This observation allowed a series of studies that showed: (1) the localization of an intramolecular disulphide bridge within the helical domain of the molecule, (2) the alignment of major peptic-digest fragments of the alpha 1 (IV) chain, and (3) confirmation of the postulated antiparallel arrangement of individual molecules within type IV collagen tetramers.
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex / Q000032:analysis; D001485:Basement Membrane / Q000032:analysis; D001665:Binding Sites; D003094:Collagen / Q000276:immunology*; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000032:analysis
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D046911:Macromolecular Substances; D010446:Peptide Fragments; D003094:Collagen