Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene.

Abstract

Research Article1 July 1985free access Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. A.R. Kornblihtt A.R. Kornblihtt Search for more papers by this author K. Umezawa K. Umezawa Search for more papers by this author K. Vibe-Pedersen K. Vibe-Pedersen Search for more papers by this author F.E. Baralle F.E. Baralle Search for more papers by this author A.R. Kornblihtt A.R. Kornblihtt Search for more papers by this author K. Umezawa K. Umezawa Search for more papers by this author K. Vibe-Pedersen K. Vibe-Pedersen Search for more papers by this author F.E. Baralle F.E. Baralle Search for more papers by this author Author Information A.R. Kornblihtt, K. Umezawa, K. Vibe-Pedersen and F.E. Baralle The EMBO Journal (1985)4:1755-1759https://doi.org/10.1002/j.1460-2075.1985.tb03847.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Cellular and plasma fibronectins are heterodimers consisting of similar but not identical polypeptides. The differences between fibronectin subunits are due in part to the variability of internal primary sequences. This results from alternative splicing in at least two regions (ED and IIICS) of the pre-mRNA. The complete primary structure of human fibronectin, including most of the internal variations, has been determined by sequencing a series of overlapping cDNA clones. In total, they covered 7692 nucleotides and represented the mRNA sequence coding from the amino terminus of the mature protein to the poly(A) tail. The deduced amino acid sequence of fibronectin has been analysed in terms of the arrangement of internal homologies and the different binding domains. Previous ArticleNext Article Volume 4Issue 71 July 1985In this issue RelatedDetailsLoading ...