| Abstract: | Two monoclonal antibodies have been characterized as being against avian type VI collagen. By competition ELISA, the antibodies bound to the native type VI collagen molecule but not to its separated chains or to any of the other native collagen types tested. By rotary shadowing analysis of complexes of antibody-type VI collagen monomers, one of the antibodies (VI-EC6) has been shown to bind to a site in the triple helical domain of the molecule. The site at which this antibody binds to the dimeric form of type VI collagen is consistent with the previously proposed model for a supramolecular organization of the molecule (Furthmayr et al., Biochem j 211 (1983) 303) in which the monomers are arranged in an antiparallel, slightly staggered overlap. Immunofluorescence analyses of sections of chicken eyes and skeletal muscle demonstrate that type VI collagen is a major component of most stromal matrices. |
