Differences in domain structure between pericellular matrix and plasma fibronectins as revealed by domain-specific antibodies combined with limited proteolysis and S-cyanylation: a preliminary note.
Differences in domain structure between human fibronectins obtained from pericellular matrix and plasma have been revealed by limited proteolysis and S-cyanylation, followed by identification of each domain with domain-specific antibodies. Although the overall domain structure is similar between pericellular and plasma fibronectins, the fragments derived from the COOH-terminal region of these fibronectins, which were defined by specific antibodies, exhibited clear differences in their molecular weights and protease susceptibility, suggesting that the structure near the COOH-terminal region is significantly different between these two proteins.
D000906:Antibodies / Q000276:immunology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005353:Fibronectins / Q000276:immunology; D006801:Humans; D007158:Immunologic Techniques; D013820:Thermolysin / Q000378:metabolism; D013861:Thiocyanates; D014357:Trypsin / Q000378:metabolism
D000906:Antibodies; D005353:Fibronectins; D013861:Thiocyanates; D014357:Trypsin; D013820:Thermolysin; C008658:2-nitro-5-thiocyanobenzoic acid