Production and characterization of a monoclonal antibody to chicken type I collagen.

AUTOR(ES)

Linsenmayer, T F

RESUMO

We have shown that lymphocyte-myeloma cell hybridization can be used to produce large amounts of extremely high-titer specific antibodies against type I collagen, a macromolecule normally of low immunogenicity. In a passive hemagglutination assay the antibody had a high titer against chicken type I collagen but showed no activity against chicken type II or rat type I collagen. By using a two-step fluorescence histochemical procedure on sections of embryonic chicken tibia, strong fluorescence was observed in the perichondrium and surrounding connective tissue (known to contain type I collagen) but not over the cartilage (characterized by type II collagen). When used in conjunction with Staphylococcus aureus as a solid phase immunoadsorbant, the antibody was shown to bind to labeled collagen synthesized in vitro by embryonic chicken calvaria.

Documentos Relacionados

• Cloning, characterization, and functional studies of a nonintegrin platelet receptor for type I collagen.
• Isolation and characterization of genomic DNA coding for alpha 2 type I collagen.
• Granulocyte collagenase: selective digestion of type I relative to type III collagen.
• Organization of collagen types I and V in the embryonic chicken cornea: monoclonal antibody studies.
• Native type II collagen-induced arthritis in the rat. I. Incidence and humoral response to collagen.