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PubMed · 3399792

[Highly purified, functionally active human fibronectin preparation].

V Regnault·C Rivat·M Maugras·J F Stoltz
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Abstract

Fibronectin has been purified by gelatin-Sepharose affinity chromatography from fresh frozen human plasma. The bound fibronectin was eluted with 3 M urea. The purity of the fibronectin obtained has been checked on (immunoelectrophoresis, polyacrylamide gel electrophoresis, FPLC). Biological activity of the purified molecule has been monitored by means of three assays: quantitation of the gelatin-binding activity by ELISA, quantitation of the fibronectin-mediated attachment of fibroblasts on plastic and evaluation of the opsonic activity (uptake of gelatin latex particles by a murine macrophage line). When deep-frozen, fibronectin retains all of its properties. This highly purified and functional fibronectin fulfills the basic requirements for a standard reagent. It will allow to investigate physicochemical and functional alterations of various fibronectins.

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Cell AdhesionChromatography, GelElectrophoresis, Polyacrylamide GelFibronectinsGelatinHumansImmunoelectrophoresis, Two-DimensionalLatex Fixation TestsOpsonin ProteinsEnglish AbstractJournal Article

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V Regnault, C Rivat, M Maugras, J F Stoltz. 1988. [Highly purified, functionally active human fibronectin preparation].. https://doi.org/10.1016/s0338-4535(88)80064-3

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