Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies

D. E. Smith, Leo T Furcht

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Monoclonal antibodies to human plasma fibronectin were used to study the topological arrangement of several biologically active sites on the 220,000-dalton fibronectin subunit. Plasma fibronectin was cleaved into a number of biologically active fragments by trypsin and cathepsin D. Fragments that bind gelatin and heparin and bind to both gelatin and heparin were isolated by affinity chromatograpy. These fragments were further characterized by their ability to bind to two different monoclonal antibodies: monoclonal 2-8 and monoclonal 180-8. Using this approach, we have established the positions of two unique heparin-, a gelatin-, and two monoclonal antibody-binding sites on the fibronectin subunit.

Original languageEnglish (US)
Pages (from-to)6518-6523
Number of pages6
JournalJournal of Biological Chemistry
Volume257
Issue number11
StatePublished - Dec 1 1982

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Plasma (human)
Fibronectins
Heparin
Gelatin
Monoclonal Antibodies
Antibody Binding Sites
Cathepsin D
Trypsin
Catalytic Domain
Plasmas

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Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies. / Smith, D. E.; Furcht, Leo T.

In: Journal of Biological Chemistry, Vol. 257, No. 11, 01.12.1982, p. 6518-6523.

Research output: Contribution to journalArticle

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