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Structural studies of human basement-membrane collagen with the use of a monoclonal antibody.

Authors
  • Dieringer, H
  • Hollister, D W
  • Glanville, R W
  • Sakai, L Y
  • Kühn, K
Type
Published Article
Journal
The Biochemical journal
Publication Date
Apr 01, 1985
Volume
227
Issue
1
Pages
217–222
Identifiers
PMID: 3994683
Source
Medline
License
Unknown

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 fragments of the alpha 1 (IV) chain, and (3) confirmation of the postulated antiparallel arrangement of individual molecules within type IV collagen tetramers.

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