Independence of reciprocal attachment sites on denatured collagen and fibronectin from antigenic sites, and binding of gelatin-based plasma substitutes to plasma fibronectin.
Fibronectin and denatured collagen possess attachment sites for each other and, in addition, antigenic sites reacting with the respective antibodies. Using an enzyme linked immunosorbent assay it was shown that attachment sites and antigenic sites on fibronectin and on collagen reacted independently of each other. Gelatin-based plasma substitutes blocked the binding of fibronectin to denatured collagen thus showing that attachment sites for fibronectin are preserved in the gelatin preparations used for manufacturing these plasma substitutes. Antigenic sites, in contrast, were destroyed during the manufacturing process as shown with antibodies to denatured collagen raised in guinea-pigs. It is concluded that complex formation of gelatin-based plasma substitutes with plasma fibronectin may occur upon infusion of such plasma substitutes but that formation of antigen/antibody complexes in vivo is unlikely.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003094:Collagen / Q000276:immunology / Q000378:metabolism*; D000939:Epitopes / Q000276:immunology*; D005260:Female; D005353:Fibronectins / Q000276:immunology / Q000378:metabolism*; D005780:Gelatin; D006168:Guinea Pigs; D006801:Humans; D007163:Immunosorbent Techniques; D010952:Plasma Substitutes / Q000378:metabolism*; D011247:Pregnancy; D011817:Rabbits
D000939:Epitopes; D005353:Fibronectins; D010952:Plasma Substitutes; D005780:Gelatin; D003094:Collagen