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. 1983 Oct 1;215(1):147–151. doi: 10.1042/bj2150147

Monoclonal antibody against the N-terminal end of human plasma fibronectin.

T Vartio, E M Salonen, G De Petro, S Barlati, V Miggiano, C Stähli, G Virgallita, B Takács, A Vaheri
PMCID: PMC1152374  PMID: 6194791

Abstract

Purified human plasma fibronectin was digested with cathepsin G and the degradation products were tested for reactivity towards a monoclonal antibody. In an immunoblotting assay, after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the digestion products, the 85 000-Mr and 72 000-Mr gelatin- and heparin-binding fragments as well as the N-terminal 30 000-Mr heparin-binding fragment reacted with the antibody, whereas the 64 000-Mr gelatin- and heparin-binding fragment did not. In enzyme immunoassay the antibody reacted with intact fibronectin and the 30 000-Mr fragment but not with a 40 000-Mr gelatin-binding fragment. The alignment of the binding domains in these fragments and in the intact molecule [Vartio (1982) Eur. J. Biochem. 123, 223-233] localizes the antigenic determinant to the 21 000 Da N-terminal Staphylococcus aureus-binding region of fibronectin.

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Selected References

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