Abstract：
:Proteolytic fragments of human plasma fibronectin were used to identify monoclonal antibodies reacting with the various domains of fibronectin. One of these antibodies, which reacts with cell-attachment-promoting fragments of fibronectin, inhibits attachment of cells to fibronectin-coated surfaces. A cell-attachment-promoting, chymotryptic, 120 kilodalton fragment was cleaved further with pepsin into three main fragments. The smallest, 15 kilodalton fragment was purified by affinity chromatography on the cell-attachment-inhibiting antibody insolubilized on Sepharose. This fragment is active in promoting cell attachment but lacks the other known binding activities of fibronectin. It can be localized between the collagen-binding and heparin-binding domains, about 127 to 197 kilodaltons from the NH2 terminus of the polypeptide. These results show that the interaction of fibronectin with cells is restricted to a defined portion of the molecule and is independent of the direct involvement of the known affinities toward other macromolecules.
journal_name
Celljournal_title
Cellauthors
Pierschbacher MD,Hayman EG,Ruoslahti Edoi
10.1016/0092-8674(81)90308-1subject
Has Abstractpub_date
1981-10-01 00:00:00pages
259-67issue
2 Pt 2eissn
0092-8674issn
1097-4172pii
0092-8674(81)90308-1journal_volume
26pub_type
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