Abstract

The proliferation promoting activity of various proteolytic fragments of human plasma fibronectin was assayed. Study of this activity in fragments, purified by affinity chromatography, has shown that only heparin-binding fragments were capable of promoting fibroblast proliferation while gelatin- and fibrin-binding fragments were not. Heparin-binding fragments with high affinity for heparin were characterized by high activity levels while those with low heparin affinity were inactive. Heparin-binding fragments with the highest proliferation promoting activity contained the cell-binding domain and were virtually devoid of the hep2, hep1 and gelatin-binding domains.

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