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
- 1 February 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 241 (3) , 923-928
- https://doi.org/10.1042/bj2410923
Abstract
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.This publication has 15 references indexed in Scilit:
- Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin.Journal of Biological Chemistry, 1985
- Primary structure of human plasma fibronectin — Characterization of the 6,000 dalton C-terminal fragment containing the interchain disulfide bridgesBiochemical and Biophysical Research Communications, 1984
- Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain.Journal of Biological Chemistry, 1983
- Biochemical and immunological characterization of three binding sites on human plasma fibronectin with different affinities for heparinBiochemistry, 1983
- Domain structure of human plasma fibronectin. Differences and similarities between human and hamster fibronectins.Journal of Biological Chemistry, 1983
- Domain structure of the carboxyl-terminal half of human plasma fibronectin.Journal of Biological Chemistry, 1983
- Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies.Journal of Biological Chemistry, 1982
- Divalent cation modulation of fibronectin binding to heparin and to DNA.Journal of Biological Chemistry, 1982
- NH2-terminal sequences of DNA-, heparin-, and gelatin-binding tryptic fragments from human plasma fibronectinArchives of Biochemistry and Biophysics, 1982
- Cleavage of tryptophanyl peptide bonds in cytochrome b5 by cyanogen bromide.Journal of Biological Chemistry, 1977