Structural analysis of fibronectin and its collagen-binding fragment from several cell lines.
Tryptic peptide mapping of fibronectin from various species indicates that (i) there exists a remarkable similarity between methionine-labeled tryptic peptides of fibronectins isolated from cells of widely separated species such as human, chicken, mouse, hamster, and rat; (ii) fibronectins from normal and transformed or tumor cells of the same species are very similar, if not identical; and (iii) collagen-binding regions of fibronectin from different species share identical major peptides.
D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004622:Embryo, Mammalian; D005347:Fibroblasts / Q000032:analysis; D005353:Fibronectins / Q000302:isolation & purification*; D006801:Humans; D007668:Kidney; D051379:Mice; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D014357:Trypsin; D001749:Urinary Bladder Neoplasms
D005353:Fibronectins; D010446:Peptide Fragments; D003094:Collagen; D014357:Trypsin