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[A simple and effective step in the purification of bovine blood fibronectin]
Preparations of fibronectin from bovine blood serum, obtained by means of affinity chromatography on collagen-Sepharose, contained immunoglobulins and other proteins, concentration of which constituted 48 +/- 5%. Differential salting out of fibronectin and other non-fibronectin proteins, using 0.8-2.0 M ammonium sulfate at pH 5.0, demonstrated that precipitation of fibronectin occurred more effectively as compared with non-fibronectin proteins at all the salt concentrations studied. If 0.8 M or 1.0 M ammonium sulfate concentrations were used, the fibronectin preparations contained less than 10% of other proteins and fibronectin loss was about 20%. Salting out of fibronectin is an effective additional step of its purification.
Preparations of fibronectin from bovine blood serum, obtained by means of affinity chromatography on collagen-Sepharose, contained immunoglobulins and other proteins, concentration of which constituted 48 +/- 5%. Differential salting out of fibronectin and other non-fibronectin proteins, using 0.8-2.0 M ammonium sulfate at pH 5.0, demonstrated that precipitation of fibronectin occurred more effectively as compared with non-fibronectin proteins at all the salt concentrations studied. If 0.8 M or 1.0 M ammonium sulfate concentrations were used, the fibronectin preparations contained less than 10% of other proteins and fibronectin loss was about 20%. Salting out of fibronectin is an effective additional step of its purification.