Differences in domain structure between pericellular matrix and plasma fibronectins as revealed by domain-specific antibodies combined with limited proteolysis and S-cyanylation: a preliminary note

Biochem Biophys Res Commun. 1983 Oct 31;116(2):534-40. doi: 10.1016/0006-291x(83)90556-9.

Abstract

Differences in domain structure between human fibronectins obtained from pericellular matrix and plasma have been revealed by limited proteolysis and S-cyanylation, followed by identification of each domain with domain-specific antibodies. Although the overall domain structure is similar between pericellular and plasma fibronectins, the fragments derived from the COOH-terminal region of these fibronectins, which were defined by specific antibodies, exhibited clear differences in their molecular weights and protease susceptibility, suggesting that the structure near the COOH-terminal region is significantly different between these two proteins.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies / immunology
  • Chemical Phenomena
  • Chemistry, Physical
  • Fibronectins* / immunology
  • Humans
  • Immunologic Techniques
  • Thermolysin / metabolism
  • Thiocyanates
  • Trypsin / metabolism

Substances

  • Antibodies
  • Fibronectins
  • Thiocyanates
  • Trypsin
  • Thermolysin
  • 2-nitro-5-thiocyanobenzoic acid