Abstract
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 fragment of the α1(IV) chain, and (3) confirmation of the postulated antiparallel arrangement of individual molecules within type IV collagen tetramers.
Original language | English (US) |
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Pages (from-to) | 217-222 |
Number of pages | 6 |
Journal | Biochemical Journal |
Volume | 227 |
Issue number | 1 |
DOIs | |
State | Published - 1985 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology