Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand.

Published

Journal Article

We have determined the structure of plasma fibronectin by electron microscopy of shadowed specimens. the 440,000 molecular weight, dimeric molecule appears to be a long, thin, highly flexible strand. The contour length of the most extended molecules is 160 nm, but a distribution of lengths down to 120 nm was observed, indicating flexibility in extension as well as in bending. The average diameter of the strand is 2 nm and there are no large globular domains. the large fragments produced by limited digestion with plasmin are not globular domains but are segments of the strand, whose length corresponds to the molecular weight of the polypeptide chain. We conclude that each polypeptide chain of the dimeric molecule spans half the length of the strand, with their carboxyl termini joined at the center of the strand and their amino termini at the ends. This model is supported by images of fibronectin-fibrinogen complexes, in which the fibrinogen is always attached to an end of the fibronectin strand.

Full Text

Duke Authors

Cited Authors

  • Erickson, HP; Carrell, N; McDonagh, J

Published Date

  • December 1, 1981

Published In

Volume / Issue

  • 91 / 3 Pt 1

Start / End Page

  • 673 - 678

PubMed ID

  • 7328116

Pubmed Central ID

  • 7328116

Electronic International Standard Serial Number (EISSN)

  • 1540-8140

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.91.3.673

Language

  • eng