title: Hydrophobic properties of porcine fibronectin and its functional domains.
abstract: The relations between surface hydrophobicities and binding properties of the functional domains of porcine plasma fibronectin were investigated. Porcine plasma fibronectin as well as human plasma fibronectin was adsorbed on a hydrophobic column with butyl or phenyl ligands in the presence of 0.5 M ammonium sulfate, and recovered in a single peak by decreasing the concentration of ammonium sulfate to 0 M, indicating that both fibronectins have very high surface hydrophobicities. On digestion with thermolysin, porcine plasma fibronectin yielded five fragments (140-150, 43, 25, 17, and 14 kDa) similar to those reported for human fibronectin, although porcine fibronectin was more resistant to the digestion than human fibronectin. The three heparin-binding fragments were found to have a wide range of surface hydrophobicities, the 140-150 kDa fragment having the lowest, the 25 kDa fragment a higher, and the 14 kDa fragment the highest among all the fragments. The 43 kDa collagen-binding and 17 kDa fragments had surface hydrophobicities as high as that of fibronectin. It is noteworthy that the 43 kDa collagen-binding fragment contributes to the high surface hydrophobicity of intact fibronectin in spite of the high content of carbohydrates.
authors.affiliation: Department of Chemistry, Faculty of Science, Ochanomizu University, Tokyo.
authors.forename: A
authors.initials: A
authors.lastname: Hayashi-Nagai
authors.forename: H
authors.initials: H
authors.lastname: Kitagaki-Ogawa
authors.forename: I
authors.initials: I
authors.lastname: Matsumoto
authors.forename: M
authors.initials: M
authors.lastname: Hayashi
authors.forename: N
authors.initials: N
authors.lastname: Seno
mesh_terms: D000327:Adsorption; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002241:Carbohydrates / Q000032:analysis; D003094:Collagen / Q000378:metabolism; D005353:Fibronectins / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D011485:Protein Binding; D013552:Swine
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D005353:Fibronectins; D010446:Peptide Fragments; D003094:Collagen