Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity.
The primary structure of a 38 kDa heparin-binding domain from human plasma fibronectin has been determined. This domain contains 380 residues arranged in three type-III homology regions of approx. 90 residues each, and a 67-amino-acid C-terminal segment. This segment has been shown to be encoded by certain mRNA species only, due to alternative splicing [Kornblihtt, Vibe-Pedersen & Baralle (1984) Nucleic Acids Research 12, 5853-5868], and therefore represents a region of heterogeneity in fibronectin. Our data indicate that at least one of the constituent polypeptide chains contains this region.
D000595:Amino Acid Sequence; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D005353:Fibronectins; D006493:Heparin / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis*; D014357:Trypsin
D005353:Fibronectins; D010446:Peptide Fragments; D006493:Heparin; D014357:Trypsin