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The affinity of fibronectin for collagen was exploited in biospecific affinity chromatography of collagen. Matrices with excellent capacity and stability were obtained by coupling collagen-binding fragments of fibronectin to Sepharose. Collagen-binding tryptic (30,000 daltons) and chymotryptic (45,000 daltons) fragments, lacking the binding sites of intact fibronectin for various other substances, were coupled to Sepharose and used to chromatograph gelatin and type I collagen. Gelatin was rapidly and quantitatively bound to these matrices at 4 degrees C and 37 degrees C, while binding of type I collagen took place more slowly and was temperature dependent. The collagen did not bind at 4 degrees C but bound quantitatively at 37 degrees C if preincubated at this temperature. These results suggest that a temperature-dependent perturbation of the triple helical structure of the collagen uncovers the binding site for fibronectin, allowing the collagen to bind to the insolubilized collagen-binding fibronectin fragments. Enzyme affinity assays showed that the conformational change in the fibronectin-binding region of collagen was irreversible. Affinity chromatography on collagen-binding fragments of fibronectin could provide a method for the study of structure and function of collagens and may prove useful for the isolation of minor collagens.
E Engvall, and
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June 1992,
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April 1994,
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E Engvall, and
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March 1973,
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E Engvall, and
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E Ruoslahti
September 1994,
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E Engvall, and
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E Ruoslahti
January 1989,
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E Engvall, and
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E Ruoslahti
January 1989,
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E Engvall, and
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E Ruoslahti
February 2004,
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E Engvall, and
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E Ruoslahti
September 1988,
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E Engvall, and
M L Bell, and
E Ruoslahti
August 1976,
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E Engvall, and
M L Bell, and
E Ruoslahti
September 1980,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
