title: Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin.
abstract: The complete amino acid sequences of the heparin-, cell- and DNA-binding domains of bovine plasma fibronectin have been determined. The fragments were generated from the 170-kDa central plasmic fragment by extensive digestion with chymotrypsin, and they contain 268, 300 and 269 amino acid residues, respectively. No half-cystines or cysteines were found in these sequences. A glucosamine-based oligosaccharide group is attached to Asn-108 in the sequence of the DNA-binding domain. Only one of the three types of internal homology found in fibronectin [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137-141], namely the type III homology, occurs in these three fragments, and each of them consists of approximately three stretches of this type III homology. Part of the arrangement of peptides was derived by comparison with the partial cDNA sequence for human fibronectin recently reported [Kornblihtt et al. (1984) Nucleic Acids Res. 12, 5853-5868].
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002477:Cells / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004247:DNA; D004268:DNA-Binding Proteins / Q000097:blood*; D005353:Fibronectins / Q000097:blood*; D006493:Heparin / Q000097:blood*; D006868:Hydrolysis; D010446:Peptide Fragments / Q000097:blood; D011485:Protein Binding
chemical_list: D004268:DNA-Binding Proteins; D005353:Fibronectins; D010446:Peptide Fragments; D006493:Heparin; D004247:DNA