[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.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity / Q000379:methods; D003094:Collagen; D005353:Fibronectins / Q000097:blood* / Q000302:isolation & purification; D009994:Osmolar Concentration; D012685:Sepharose / Q000031:analogs & derivatives
D005353:Fibronectins; D003094:Collagen; D012685:Sepharose
Prostoĭ i éffektivnyĭ dopolnitel'nyĭ étap ochistki fibronektina syvorotki byka.